--- _id: '21145' abstract: - lang: eng text: 'Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. ' acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: "We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance with constructing the structural model of the IgG:GB1 complex.\r\nThis research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó and Margarita Valhondo Falcón for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01). Christophe Chipot acknowledges the European Research Council (grant project 101097272 ``MilliInMicro'') and the Métropole du Grand Nancy (grant project ``ARC''). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011." article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Christophe full_name: Chipot, Christophe last_name: Chipot citation: ama: Becker LM, Schanda P, Chipot C. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2026. doi:10.15479/AT-ISTA-21145 apa: Becker, L. M., Schanda, P., & Chipot, C. (2026). Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-21145 chicago: Becker, Lea Marie, Paul Schanda, and Christophe Chipot. “Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-21145. ieee: L. M. Becker, P. Schanda, and C. Chipot, “Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2026. ista: Becker LM, Schanda P, Chipot C. 2026. Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-21145. mla: Becker, Lea Marie, et al. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-21145. short: L.M. Becker, P. Schanda, C. Chipot, (2026). contributor: - contributor_type: researcher first_name: Haohao last_name: Fu - contributor_type: researcher first_name: Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - contributor_type: researcher first_name: Matthias last_name: Dreydoppel - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Daniel id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E last_name: Balazs orcid: 0000-0001-7597-043X - contributor_type: researcher first_name: Ulrich last_name: Weininger - contributor_type: researcher first_name: Sylvain last_name: Engilberge corr_author: '1' date_created: 2026-02-05T13:54:39Z date_published: 2026-02-09T00:00:00Z date_updated: 2026-02-18T10:04:44Z day: '09' ddc: - '572' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-21145 file: - access_level: open_access checksum: 02a419cce8cea450bc952f35488d2df5 content_type: text/plain creator: lbecker date_created: 2026-02-05T13:52:37Z date_updated: 2026-02-05T13:52:37Z file_id: '21146' file_name: README.txt file_size: 4263 relation: table_of_contents - access_level: open_access checksum: b0b82b1aa73985b0b308a3fa52d21aea content_type: application/zip creator: lbecker date_created: 2026-02-05T13:52:41Z date_updated: 2026-02-05T13:52:41Z file_id: '21147' file_name: Research_Data.zip file_size: 50647107 relation: main_file success: 1 file_date_updated: 2026-02-05T13:52:41Z has_accepted_license: '1' license: https://creativecommons.org/licenses/by-nc/4.0/ month: '02' oa: 1 oa_version: Published Version project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publisher: Institute of Science and Technology Austria related_material: record: - id: '20641' relation: earlier_version status: public status: public title: Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2026' ... --- OA_place: repository OA_type: free access _id: '21284' abstract: - lang: eng text: The advantageous characteristics attributed to the 19F nucleus have made it a popular target for NMR once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle-spinning NMR to fluorine-labeled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilized to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labeled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labeled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical-shift assignments of all four fluorotryptophan signals in the 12 × 39 kDa large protein using a mutagenesis approach. acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: We thank Ben P. Tatman for insightful discussions. This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Schanda P. Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” 2026. doi:10.15479/AT-ISTA-21284 apa: Becker, L. M., & Schanda, P. (2026). Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-21284 chicago: Becker, Lea Marie, and Paul Schanda. “Research Data for ‘Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-21284. ieee: L. M. Becker and P. Schanda, “Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.’” Institute of Science and Technology Austria, 2026. ista: Becker LM, Schanda P. 2026. Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-21284. mla: Becker, Lea Marie, and Paul Schanda. Research Data for “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-21284. short: L.M. Becker, P. Schanda, (2026). contributor: - contributor_type: researcher first_name: Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Rajkumar id: a3089acd-6806-11ee-bacc-f0c7d500ad20 last_name: Singh - contributor_type: researcher first_name: Undina id: bb74f472-ae54-11eb-9835-bc9c22fb1183 last_name: Guillerm - contributor_type: researcher first_name: Roman last_name: Lichtenecker corr_author: '1' date_created: 2026-02-17T10:17:14Z date_published: 2026-02-18T00:00:00Z date_updated: 2026-02-18T10:12:49Z day: '18' ddc: - '541' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-21284 file: - access_level: open_access checksum: 2d3105f26be578073b88ee1f2ea0bdb1 content_type: application/zip creator: lbecker date_created: 2026-02-17T10:11:14Z date_updated: 2026-02-17T10:11:14Z file_id: '21285' file_name: Research_data.zip file_size: 36996027 relation: main_file success: 1 - access_level: open_access checksum: e24aebcdb8856cb181cbaa02de020ddb content_type: text/plain creator: lbecker date_created: 2026-02-17T10:11:14Z date_updated: 2026-02-17T10:11:14Z file_id: '21286' file_name: README.txt file_size: 1993 relation: table_of_contents file_date_updated: 2026-02-17T10:11:14Z has_accepted_license: '1' month: '2' oa: 1 oa_version: None publisher: Institute of Science and Technology Austria status: public title: Research data for "Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2026' ... --- _id: '19956' abstract: - lang: eng text: The specific introduction of 1H-13C or 1H-15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a 13C-1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected arginine MAS NMR approaches to probe arginine dynamics. In experiments on crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR acknowledged_ssus: - _id: NMR - _id: LifeSc article_processing_charge: No author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Schanda P. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. 2025. doi:10.15479/AT-ISTA-19956 apa: Schanda, P. (2025). Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-19956 chicago: Schanda, Paul. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-19956. ieee: P. Schanda, “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025. ista: Schanda P. 2025. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme, Institute of Science and Technology Austria, 10.15479/AT-ISTA-19956. mla: Schanda, Paul. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-19956. short: P. Schanda, (2025). contributor: - contributor_type: researcher first_name: Darja last_name: Rohden - contributor_type: researcher first_name: Federico last_name: Napoli - contributor_type: researcher first_name: Ben last_name: Tatman - contributor_type: researcher first_name: Paul last_name: Schanda corr_author: '1' date_created: 2025-07-03T04:21:37Z date_published: 2025-07-03T00:00:00Z date_updated: 2025-12-29T14:52:16Z day: '03' ddc: - '572' department: - _id: PaSc doi: 10.15479/AT-ISTA-19956 file: - access_level: open_access checksum: a2ef61aa9fb5313c7d426913eb0482c0 content_type: application/octet-stream creator: pschanda date_created: 2025-07-03T10:30:14Z date_updated: 2025-07-03T10:30:14Z file_id: '19960' file_name: README file_size: 1160 relation: main_file success: 1 - access_level: open_access checksum: 8fb77b96d0fcc95c9903005652207a8c content_type: application/zip creator: pschanda date_created: 2025-07-03T10:30:55Z date_updated: 2025-07-03T10:30:55Z file_id: '19961' file_name: data_Arg_MASNMR_Rohden.zip file_size: 128597184 relation: main_file success: 1 - access_level: open_access checksum: a60cc16d20b089c4bef94040a99cfba5 content_type: application/x-xz creator: pschanda date_created: 2025-08-14T07:06:58Z date_updated: 2025-08-14T07:06:58Z file_id: '20172' file_name: 20240903_ubi_DN_Argd1C13_2D_spectra.tar.xz file_size: 4766564 relation: main_file success: 1 file_date_updated: 2025-08-14T07:06:58Z has_accepted_license: '1' month: '07' oa: 1 oa_version: None project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publisher: Institute of Science and Technology Austria related_material: record: - id: '20258' relation: used_in_publication status: public status: public title: Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '20184' abstract: - lang: eng text: Specialized DNA polymerases facilitate various cellular processes. Despite extensive research, the mutagenic effects of these error-prone enzymes on genomes are not fully understood. Here we show that Pol IV promotes genomic instability in Pseudomonas aeruginosa by misincorporating oxidized guanine nucleotides. This activity led to a distinctive mutational signature, characterized by A-to-C transversions occurring preferentially at AT sites flanked by a 5’G and/or 3’C. Furthermore, Pol IV preferentially targeted pathogenicity genes located at specific chromosomal locations near the replication termination region and rRNA-encoding operons. Half of the mutation events catalyzed by Pol IV impaired gene function. This can be attributed to the bias of Pol IV for mutating codons with its preferred sequence contexts, leading to substitutions to unreactive alanine and glycine residues. Remarkably, mutation signatures identified for Pol IV were found in clinical isolate genomes of P. aeruginosa, providing compelling evidence for its role in genetic diversification during pathogen adaptation. acknowledgement: "This work was supported by the Secretaría de Ciencia y Técnica (33620230100926CB), Universidad Nacional de Córdoba; and the Agencia Nacional de Promoción Científica y Técnica (PICT 2018-4527).\r\n\r\n" article_number: '1148' article_processing_charge: Yes article_type: original author: - first_name: Sofía D. full_name: Castell, Sofía D. last_name: Castell - first_name: Consuelo M. full_name: Fernandez, Consuelo M. last_name: Fernandez - first_name: Ignacio N. full_name: Tumas, Ignacio N. last_name: Tumas - first_name: Lucía M. full_name: Margara, Lucía M. last_name: Margara - first_name: Maria C full_name: Miserendino, Maria C id: 273e0cbd-72f0-11ef-b75a-f9f932e292fa last_name: Miserendino - first_name: Danilo G. full_name: Ceschin, Danilo G. last_name: Ceschin - first_name: Roberto J. full_name: Pezza, Roberto J. last_name: Pezza - first_name: Mariela R. full_name: Monti, Mariela R. last_name: Monti citation: ama: Castell SD, Fernandez CM, Tumas IN, et al. The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. Communications Biology. 2025;8. doi:10.1038/s42003-025-08589-5 apa: Castell, S. D., Fernandez, C. M., Tumas, I. N., Margara, L. M., Miserendino, M. C., Ceschin, D. G., … Monti, M. R. (2025). The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. Communications Biology. Springer Nature. https://doi.org/10.1038/s42003-025-08589-5 chicago: Castell, Sofía D., Consuelo M. Fernandez, Ignacio N. Tumas, Lucía M. Margara, Maria C Miserendino, Danilo G. Ceschin, Roberto J. Pezza, and Mariela R. Monti. “The Low-Fidelity DNA Pol IV Accelerates Evolution of Pathogenicity Genes in Pseudomonas Aeruginosa.” Communications Biology. Springer Nature, 2025. https://doi.org/10.1038/s42003-025-08589-5. ieee: S. D. Castell et al., “The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa,” Communications Biology, vol. 8. Springer Nature, 2025. ista: Castell SD, Fernandez CM, Tumas IN, Margara LM, Miserendino MC, Ceschin DG, Pezza RJ, Monti MR. 2025. The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. Communications Biology. 8, 1148. mla: Castell, Sofía D., et al. “The Low-Fidelity DNA Pol IV Accelerates Evolution of Pathogenicity Genes in Pseudomonas Aeruginosa.” Communications Biology, vol. 8, 1148, Springer Nature, 2025, doi:10.1038/s42003-025-08589-5. short: S.D. Castell, C.M. Fernandez, I.N. Tumas, L.M. Margara, M.C. Miserendino, D.G. Ceschin, R.J. Pezza, M.R. Monti, Communications Biology 8 (2025). date_created: 2025-08-17T22:01:35Z date_published: 2025-08-02T00:00:00Z date_updated: 2025-09-30T14:18:46Z day: '02' ddc: - '570' department: - _id: PaSc - _id: GradSch doi: 10.1038/s42003-025-08589-5 external_id: isi: - '001541878500001' pmid: - '40753298' has_accepted_license: '1' intvolume: ' 8' isi: 1 language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s42003-025-08589-5 month: '08' oa: 1 oa_version: Published Version pmid: 1 publication: Communications Biology publication_identifier: eissn: - 2399-3642 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 8 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20258' abstract: - lang: eng text: The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected MAS NMR approaches to probe arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR. acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: This work was supported financially by the Austrian Science Fund (FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent support of the NMR facility. article_number: '169379' article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Darja full_name: Rohden, Darja id: 81dc668a-19fa-11f0-bf31-d56534059ef3 last_name: Rohden - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - first_name: Anna full_name: Kapitonova, Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169379 apa: Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., & Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2025.169379 chicago: Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology. Elsevier, 2025. https://doi.org/10.1016/j.jmb.2025.169379. ieee: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P. Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme,” Journal of Molecular Biology, vol. 437, no. 23. Elsevier, 2025. ista: Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. 437(23), 169379. mla: Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Journal of Molecular Biology, vol. 437, no. 23, 169379, Elsevier, 2025, doi:10.1016/j.jmb.2025.169379. short: D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda, Journal of Molecular Biology 437 (2025). corr_author: '1' date_created: 2025-08-31T22:01:33Z date_published: 2025-12-01T00:00:00Z date_updated: 2025-12-29T14:52:17Z day: '01' ddc: - '540' department: - _id: PaSc doi: 10.1016/j.jmb.2025.169379 external_id: isi: - '001618289100020' file: - access_level: open_access checksum: 90d50594d8ea9860ac5da41297992847 content_type: application/pdf creator: dernst date_created: 2025-12-29T14:51:40Z date_updated: 2025-12-29T14:51:40Z file_id: '20876' file_name: 2025_JourMolecularBiology_Rohden.pdf file_size: 2270555 relation: main_file success: 1 file_date_updated: 2025-12-29T14:51:40Z has_accepted_license: '1' intvolume: ' 437' isi: 1 issue: '23' language: - iso: eng month: '12' oa: 1 oa_version: Published Version project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Journal of Molecular Biology publication_identifier: eissn: - 1089-8638 issn: - 0022-2836 publication_status: published publisher: Elsevier quality_controlled: '1' related_material: record: - id: '19956' relation: research_data status: public scopus_import: '1' status: public title: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 437 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20321' abstract: - lang: eng text: Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR. acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: The authors thank Alexey Krushelnitsky for useful discussions. C.P.J. thanks NSF (MCB-2303862) and NIH (R35GM156238 and S10OD012303) for funding. This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - first_name: Vidhyalakshmi full_name: Sridharan, Vidhyalakshmi last_name: Sridharan - first_name: Motilal full_name: Uttarkabat, Motilal last_name: Uttarkabat - first_name: Christopher P. full_name: Jaroniec, Christopher P. last_name: Jaroniec - first_name: Matthias full_name: Ernst, Matthias last_name: Ernst - first_name: Petra full_name: Rovo, Petra id: c316e53f-b965-11eb-b128-bb26acc59c00 last_name: Rovo orcid: 0000-0001-8729-7326 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Tatman B, Sridharan V, Uttarkabat M, et al. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. 2025;147(32):29315-29326. doi:10.1021/jacs.5c09057' apa: 'Tatman, B., Sridharan, V., Uttarkabat, M., Jaroniec, C. P., Ernst, M., Rovo, P., & Schanda, P. (2025). Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.5c09057' chicago: 'Tatman, Benjamin, Vidhyalakshmi Sridharan, Motilal Uttarkabat, Christopher P. Jaroniec, Matthias Ernst, Petra Rovo, and Paul Schanda. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” Journal of the American Chemical Society. American Chemical Society, 2025. https://doi.org/10.1021/jacs.5c09057.' ieee: 'B. Tatman et al., “Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR,” Journal of the American Chemical Society, vol. 147, no. 32. American Chemical Society, pp. 29315–29326, 2025.' ista: 'Tatman B, Sridharan V, Uttarkabat M, Jaroniec CP, Ernst M, Rovo P, Schanda P. 2025. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. 147(32), 29315–29326.' mla: 'Tatman, Benjamin, et al. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” Journal of the American Chemical Society, vol. 147, no. 32, American Chemical Society, 2025, pp. 29315–26, doi:10.1021/jacs.5c09057.' short: B. Tatman, V. Sridharan, M. Uttarkabat, C.P. Jaroniec, M. Ernst, P. Rovo, P. Schanda, Journal of the American Chemical Society 147 (2025) 29315–29326. corr_author: '1' date_created: 2025-09-10T05:37:19Z date_published: 2025-08-01T00:00:00Z date_updated: 2026-01-28T12:36:30Z day: '01' ddc: - '540' department: - _id: PaSc - _id: NMR doi: 10.1021/jacs.5c09057 external_id: isi: - '001542746200001' pmid: - '40748291' file: - access_level: open_access checksum: b350d56ddddefea96cebd62c277c0ff5 content_type: application/pdf creator: dernst date_created: 2025-09-10T07:53:10Z date_updated: 2025-09-10T07:53:10Z file_id: '20337' file_name: 2025_JACS_Tatman.pdf file_size: 5235353 relation: main_file success: 1 file_date_updated: 2025-09-10T07:53:10Z has_accepted_license: '1' intvolume: ' 147' isi: 1 issue: '32' language: - iso: eng month: '08' oa: 1 oa_version: Published Version page: 29315-29326 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' related_material: record: - id: '19696' relation: used_in_publication status: public scopus_import: '1' status: public title: 'Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 147 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20538' abstract: - lang: eng text: In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins. acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B. This work was supported financially by the Austrian Science Fund (FWF, grant numbers I06223 and I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Celina Sailer for assistance with the analysis of the NMR spectrum of HsTom70. article_number: '169465' article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Sonja full_name: Knödlstorfer, Sonja last_name: Knödlstorfer - first_name: Giorgia full_name: Toscano, Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - first_name: Aleksandra L. full_name: Ptaszek, Aleksandra L. last_name: Ptaszek - first_name: Georg full_name: Kontaxis, Georg last_name: Kontaxis - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - first_name: Jakob full_name: Schneider, Jakob id: 64368429-eb97-11eb-a6c2-c980b1f44415 last_name: Schneider - first_name: Katharina full_name: Maier, Katharina last_name: Maier - first_name: Anna full_name: Kapitonova, Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Robert full_name: Konrat, Robert last_name: Konrat citation: ama: Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169465 apa: Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider, J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2025.169465 chicago: Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis, Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” Journal of Molecular Biology. Elsevier, 2025. https://doi.org/10.1016/j.jmb.2025.169465. ieee: S. Knödlstorfer et al., “A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0,” Journal of Molecular Biology, vol. 437, no. 23. Elsevier, 2025. ista: Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J, Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465. mla: Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” Journal of Molecular Biology, vol. 437, no. 23, 169465, Elsevier, 2025, doi:10.1016/j.jmb.2025.169465. short: S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider, K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of Molecular Biology 437 (2025). date_created: 2025-10-26T23:01:35Z date_published: 2025-12-01T00:00:00Z date_updated: 2025-12-30T10:29:20Z day: '01' ddc: - '540' department: - _id: PaSc - _id: GradSch doi: 10.1016/j.jmb.2025.169465 external_id: pmid: - '41016549' file: - access_level: open_access checksum: feb92f9c79032c261165f4ca573f444a content_type: application/pdf creator: dernst date_created: 2025-12-30T10:29:08Z date_updated: 2025-12-30T10:29:08Z file_id: '20915' file_name: 2025_JourMolecularBiology_Knoedlstorfer.pdf file_size: 3076611 relation: main_file success: 1 file_date_updated: 2025-12-30T10:29:08Z has_accepted_license: '1' intvolume: ' 437' issue: '23' language: - iso: eng month: '12' oa: 1 oa_version: Published Version pmid: 1 project: - _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0 grant_number: I06223 name: Structure and mechanism of the mitochondrial MIM insertase - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Journal of Molecular Biology publication_identifier: eissn: - 1089-8638 issn: - 0022-2836 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0 tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 437 year: '2025' ... --- OA_type: free access _id: '20641' abstract: - lang: eng text: 'Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. ' acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: "We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance with constructing the structural model of the IgG:GB1 complex.\r\nThis research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó and Margarita Valhondo Falcón for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01). Christophe Chipot acknowledges the European Research Council (grant project 101097272 ``MilliInMicro'') and the Métropole du Grand Nancy (grant project ``ARC''). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011." article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Schanda P. Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2025. doi:10.15479/AT-ISTA-20641 apa: Becker, L. M., & Schanda, P. (2025). Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20641 chicago: Becker, Lea Marie, and Paul Schanda. “Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20641. ieee: L. M. Becker and P. Schanda, “Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2025. ista: Becker LM, Schanda P. 2025. Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-20641. mla: Becker, Lea Marie, and Paul Schanda. Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-20641. short: L.M. Becker, P. Schanda, (2025). contributor: - contributor_type: researcher first_name: 'Haohao ' last_name: Fu - contributor_type: researcher first_name: Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - contributor_type: researcher first_name: Matthias last_name: Dreydoppel - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Daniel id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E last_name: Balazs orcid: 0000-0001-7597-043X - contributor_type: researcher first_name: Ulrich last_name: Weininger - contributor_type: researcher first_name: Sylvain last_name: Engilberge - contributor_type: researcher first_name: Christophe last_name: Chipot corr_author: '1' date_created: 2025-11-13T09:29:58Z date_published: 2025-11-18T00:00:00Z date_updated: 2026-02-18T10:04:45Z day: '18' ddc: - '572' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-20641 file: - access_level: open_access checksum: a73a0550c644957e7f62241e239d3a1d content_type: application/zip creator: lbecker date_created: 2025-11-13T09:38:35Z date_updated: 2026-02-17T10:16:57Z file_id: '20643' file_name: Research_Data.zip file_size: 1806589513 relation: main_file - access_level: open_access checksum: 7176b257f753c213a0460ee06f802363 content_type: application/pdf creator: lbecker date_created: 2025-11-17T11:54:17Z date_updated: 2026-02-17T10:16:57Z file_id: '20652' file_name: README.pdf file_size: 191376 relation: table_of_contents file_date_updated: 2026-02-17T10:16:57Z has_accepted_license: '1' month: '11' oa: 1 oa_version: None project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publisher: Institute of Science and Technology Austria related_material: record: - id: '21145' relation: later_version status: public status: public title: Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- OA_type: closed access _id: '19072' abstract: - lang: eng text: Pathogenic fungal and bacterial cells are enveloped within a cell wall, a molecular barrier at their cell surface, and a critical architecture that constantly evolves during pathogenesis. Understanding the molecular composition, structural organization, and mobility of polysaccharides constituting this cell envelope is crucial to correlate cell wall organization with its role in pathogenicity and to identify potential antifungal targets. For the fungal pathogen Cryptococcus neoformans, the characterization of the cell envelope has been complexified by the presence of an additional external polysaccharide capsular shell. Here, we investigate how magic-angle spinning (MAS) solid-state NMR techniques increase the analytical capabilities to characterize the structure and dynamics of this encapsulated pathogen. The versatility of proton detection experiments, dynamic-based filters, and relaxation measurements facilitate the discrimination of the highly mobile external capsular structure from the internal rigid cell wall of C. neoformans. In addition, we report the in situ detection of triglyceride molecules from lipid droplets based on NMR dynamic filters. Together, we demonstrate a nondestructive technique to study the cell wall architecture of encapsulated microbes using C. neoformans as a model, an airborne opportunistic fungal pathogen that infects mainly immunocompromised but also competent hosts. acknowledgement: We thank the ANR (ANR-16-CE11-0020-02 to A. Loquet, and V.A. and ANR-21-CE17-0032-01 grant FUNPOLYVAC to V.A.) as well as the Swiss National Science Foundation for early postdoc mobility project P2EZP2_184258 to A. Lends. This work has benefited from the Biophysical and Structural Chemistry Platform at Institut Européen de Chimie et Biologie IECB, Centre National de la Recherche Scientifique CNRS Unité d’Appui et de Recherche UAR 3033, INSERM US001, and CNRS (IR-RMN FR3050 and Infranalytics FR2054). article_processing_charge: No article_type: original author: - first_name: Alons full_name: Lends, Alons last_name: Lends - first_name: Gaelle full_name: Lamon, Gaelle last_name: Lamon - first_name: Loic full_name: Delcourte, Loic last_name: Delcourte - first_name: Aude full_name: Sturny-Leclere, Aude last_name: Sturny-Leclere - first_name: Axelle full_name: Grélard, Axelle last_name: Grélard - first_name: Estelle full_name: Morvan, Estelle last_name: Morvan - first_name: Muhammed Bilal full_name: Abdul-Shukkoor, Muhammed Bilal last_name: Abdul-Shukkoor - first_name: Mélanie full_name: Berbon, Mélanie last_name: Berbon - first_name: Alicia full_name: Vallet, Alicia last_name: Vallet - first_name: Birgit full_name: Habenstein, Birgit last_name: Habenstein - first_name: Erick J. full_name: Dufourc, Erick J. last_name: Dufourc - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Vishukumar full_name: Aimanianda, Vishukumar last_name: Aimanianda - first_name: Antoine full_name: Loquet, Antoine last_name: Loquet citation: ama: Lends A, Lamon G, Delcourte L, et al. Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. Journal of the American Chemical Society. 2025;147(8):6813-6824. doi:10.1021/jacs.4c16975 apa: Lends, A., Lamon, G., Delcourte, L., Sturny-Leclere, A., Grélard, A., Morvan, E., … Loquet, A. (2025). Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.4c16975 chicago: Lends, Alons, Gaelle Lamon, Loic Delcourte, Aude Sturny-Leclere, Axelle Grélard, Estelle Morvan, Muhammed Bilal Abdul-Shukkoor, et al. “Molecular Distinction of Cell Wall and Capsular Polysaccharides in Encapsulated Pathogens by in Situ Magic-Angle Spinning NMR Techniques.” Journal of the American Chemical Society. American Chemical Society, 2025. https://doi.org/10.1021/jacs.4c16975. ieee: A. Lends et al., “Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques,” Journal of the American Chemical Society, vol. 147, no. 8. American Chemical Society, pp. 6813–6824, 2025. ista: Lends A, Lamon G, Delcourte L, Sturny-Leclere A, Grélard A, Morvan E, Abdul-Shukkoor MB, Berbon M, Vallet A, Habenstein B, Dufourc EJ, Schanda P, Aimanianda V, Loquet A. 2025. Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. Journal of the American Chemical Society. 147(8), 6813–6824. mla: Lends, Alons, et al. “Molecular Distinction of Cell Wall and Capsular Polysaccharides in Encapsulated Pathogens by in Situ Magic-Angle Spinning NMR Techniques.” Journal of the American Chemical Society, vol. 147, no. 8, American Chemical Society, 2025, pp. 6813–24, doi:10.1021/jacs.4c16975. short: A. Lends, G. Lamon, L. Delcourte, A. Sturny-Leclere, A. Grélard, E. Morvan, M.B. Abdul-Shukkoor, M. Berbon, A. Vallet, B. Habenstein, E.J. Dufourc, P. Schanda, V. Aimanianda, A. Loquet, Journal of the American Chemical Society 147 (2025) 6813–6824. date_created: 2025-02-23T23:01:56Z date_published: 2025-02-16T00:00:00Z date_updated: 2025-09-30T10:36:53Z day: '16' department: - _id: PaSc doi: 10.1021/jacs.4c16975 external_id: isi: - '001423628600001' pmid: - '39955787' intvolume: ' 147' isi: 1 issue: '8' language: - iso: eng month: '02' oa_version: None page: 6813-6824 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 147 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '19555' abstract: - lang: eng text: The charged arginine side chain is unique in determining many innate properties of proteins, contributing to stability and interaction surfaces, and directing allosteric regulation and enzymatic catalysis. NMR experiments can be used to reveal these processes at the molecular level, but it often requires selective insertion of carbon-13, nitrogen-15, and deuterium at defined atomic positions. We introduce a method to endow arginine residues with defined isotope patterns, combining synthetic organic chemistry and cell-based protein overexpression. The resulting proteins feature NMR active spin systems with optimized relaxation pathways leading to simplified NMR spectra with a sensitive response to changes in the chemical environment of the nuclei observed. acknowledged_ssus: - _id: NMR acknowledgement: We thank Lea Marie Becker for assistance with python scripts used to analyze the labeling efficiency, and Undina Guillerm, Rajkumar Singh, and Anna Kapitonova for help with protein production. This work was supported by the Austrian Science Fund (FWF; project number I5812-B) through a French-Austrian bi-national research project. We thank the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the NMR Facility, as well as the NMR center and MS center of the University of Vienna. article_number: e202500408 article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Darja full_name: Rohden, Darja id: 81dc668a-19fa-11f0-bf31-d56534059ef3 last_name: Rohden - first_name: Giorgia full_name: Toscano, Giorgia last_name: Toscano - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker citation: ama: Rohden D, Toscano G, Schanda P, Lichtenecker RJ. Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. Chemistry - A European Journal. 2025;31(24). doi:10.1002/chem.202500408 apa: Rohden, D., Toscano, G., Schanda, P., & Lichtenecker, R. J. (2025). Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. Chemistry - A European Journal. Wiley. https://doi.org/10.1002/chem.202500408 chicago: Rohden, Darja, Giorgia Toscano, Paul Schanda, and Roman J. Lichtenecker. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” Chemistry - A European Journal. Wiley, 2025. https://doi.org/10.1002/chem.202500408. ieee: D. Rohden, G. Toscano, P. Schanda, and R. J. Lichtenecker, “Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy,” Chemistry - A European Journal, vol. 31, no. 24. Wiley, 2025. ista: Rohden D, Toscano G, Schanda P, Lichtenecker RJ. 2025. Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. Chemistry - A European Journal. 31(24), e202500408. mla: Rohden, Darja, et al. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” Chemistry - A European Journal, vol. 31, no. 24, e202500408, Wiley, 2025, doi:10.1002/chem.202500408. short: D. Rohden, G. Toscano, P. Schanda, R.J. Lichtenecker, Chemistry - A European Journal 31 (2025). corr_author: '1' date_created: 2025-04-13T22:01:19Z date_published: 2025-04-25T00:00:00Z date_updated: 2025-09-30T11:35:05Z day: '25' ddc: - '540' department: - _id: PaSc doi: 10.1002/chem.202500408 external_id: isi: - '001479486400019' pmid: - '40080421' file: - access_level: open_access checksum: e3788628644b5aac666cf079b05f8fa7 content_type: application/pdf creator: dernst date_created: 2025-08-05T12:59:24Z date_updated: 2025-08-05T12:59:24Z file_id: '20136' file_name: 2025_ChemistryEur_Rohden.pdf file_size: 2840681 relation: main_file success: 1 file_date_updated: 2025-08-05T12:59:24Z has_accepted_license: '1' intvolume: ' 31' isi: 1 issue: '24' language: - iso: eng month: '04' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Chemistry - A European Journal publication_identifier: eissn: - 1521-3765 issn: - 0947-6539 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 31 year: '2025' ... --- _id: '19696' acknowledged_ssus: - _id: NMR - _id: LifeSc article_processing_charge: No author: - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman citation: ama: 'Tatman B. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” 2025. doi:10.15479/AT-ISTA-19696' apa: 'Tatman, B. (2025). Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-19696' chicago: 'Tatman, Benjamin. “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-19696.' ieee: 'B. Tatman, “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.’” Institute of Science and Technology Austria, 2025.' ista: 'Tatman B. 2025. Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-19696.' mla: 'Tatman, Benjamin. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-19696.' short: B. Tatman, (2025). contributor: - contributor_type: project_leader first_name: Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - contributor_type: researcher first_name: Vidhyalakshmi last_name: Sridharan - contributor_type: researcher first_name: Motilal last_name: Uttarkabat - contributor_type: researcher first_name: Christopher last_name: Jaroniec - contributor_type: researcher first_name: Matthias last_name: Ernst - contributor_type: researcher first_name: Petra id: c316e53f-b965-11eb-b128-bb26acc59c00 last_name: Rovo orcid: 0000-0001-8729-7326 corr_author: '1' date_created: 2025-05-14T10:46:07Z date_published: 2025-07-31T00:00:00Z date_updated: 2026-01-28T12:36:30Z day: '31' department: - _id: PaSc doi: 10.15479/AT-ISTA-19696 file: - access_level: open_access checksum: 4c2d29404e070bda7d5619f728ec555c content_type: application/zip creator: btatman date_created: 2025-07-31T08:14:40Z date_updated: 2025-07-31T08:14:40Z file_id: '20094' file_name: dataset.zip file_size: 557878455 relation: main_file success: 1 - access_level: open_access checksum: 6cbccd602be0ecb6ddb1f81fdfcadf92 content_type: text/plain creator: btatman date_created: 2025-07-31T08:14:21Z date_updated: 2025-07-31T08:14:21Z file_id: '20095' file_name: readme.txt file_size: 3514 relation: main_file success: 1 file_date_updated: 2025-07-31T08:14:40Z has_accepted_license: '1' license: https://creativecommons.org/licenses/by-nc-sa/4.0/ month: '07' oa: 1 oa_version: None publisher: Institute of Science and Technology Austria related_material: link: - description: Paper to which the dataset corresponds. relation: research_paper url: http.//doi.org/10.1021/jacs.5c09057 record: - id: '20321' relation: research_data status: public status: public title: 'Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State"' tmp: image: /images/cc_by_nc_sa.png legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) short: CC BY-NC-SA (4.0) type: research_data user_id: 2EBD1598-F248-11E8-B48F-1D18A9856A87 year: '2025' ... --- OA_place: publisher OA_type: gold _id: '21327' abstract: - lang: eng text: Proteins exist as a dynamic ensemble of multiple conformations, and these motions are often crucial for their functions. However, current structure prediction methods predominantly yield a single conformation, overlooking the conformational heterogeneity revealed by diverse experimental modalities. Here, we present a framework for building experiment-grounded protein structure generative models that infer conformational ensembles consistent with measured experimental data. The key idea is to treat stateof-the-art protein structure predictors (e.g., AlphaFold3) as sequence-conditioned structural priors, and cast ensemble modeling as posterior inference of protein structures given experimental measurements. Through extensive real-data experiments, we demonstrate the generality of our method to incorporate a variety of experimental measurements. In particular, our framework uncovers previously unmodeled conformational heterogeneity from crystallographic densities, and generates high-accuracy NMR ensembles orders of magnitude faster than the status quo. Notably, we demonstrate that our ensembles outperform AlphaFold3 (Abramson et al., 2024) and sometimes better fit experimental data than publicly deposited structures to the Protein Data Bank (PDB, Burley et al. (2017)). We believe that this approach will unlock building predictive models that fully embrace experimentally observed conformational diversity. acknowledged_ssus: - _id: ScienComp acknowledgement: 'This work was supported by the Israeli Science Foundation (ISF) grant number 1834/24. We acknowledge support from the Austrian Science Fund (FWF, grant numbers I5812-B and I6223) and the financial support of the Helmsley Fellowships Program for Sustainability and Health. This research uses resources of the Institute of Science and Technology Austria’s scientific computing cluster. ' alternative_title: - PMLR article_processing_charge: No arxiv: 1 author: - first_name: Sai A full_name: Maddipatla, Sai A id: e957f5e5-91c9-11f0-a95f-e090f66ecb4d last_name: Maddipatla - first_name: Nadav E full_name: Sellam, Nadav E id: ef280fe0-91c9-11f0-a95f-8dea3f5bc513 last_name: Sellam - first_name: Meital I full_name: Bojan, Meital I id: 11d88cf5-91ca-11f0-a95f-edf9f08f47b7 last_name: Bojan - first_name: Sanketh full_name: Vedula, Sanketh id: 94f2fe44-70fa-11f0-b76b-92922c09452b last_name: Vedula - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Ailie full_name: Marx, Ailie last_name: Marx - first_name: Alexander full_name: Bronstein, Alexander id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6 last_name: Bronstein orcid: 0000-0001-9699-8730 citation: ama: 'Maddipatla SA, Sellam NE, Bojan MI, et al. Inverse problems with experiment-guided AlphaFold. In: Proceedings of the 42nd International Conference on Machine Learning. Vol 267. ML Research Press; 2025:42366-42393.' apa: 'Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Vedula, S., Schanda, P., Marx, A., & Bronstein, A. M. (2025). Inverse problems with experiment-guided AlphaFold. In Proceedings of the 42nd International Conference on Machine Learning (Vol. 267, pp. 42366–42393). Vancouver, Canada: ML Research Press.' chicago: Maddipatla, Sai A, Nadav E Sellam, Meital I Bojan, Sanketh Vedula, Paul Schanda, Ailie Marx, and Alex M. Bronstein. “Inverse Problems with Experiment-Guided AlphaFold.” In Proceedings of the 42nd International Conference on Machine Learning, 267:42366–93. ML Research Press, 2025. ieee: S. A. Maddipatla et al., “Inverse problems with experiment-guided AlphaFold,” in Proceedings of the 42nd International Conference on Machine Learning, Vancouver, Canada, 2025, vol. 267, pp. 42366–42393. ista: 'Maddipatla SA, Sellam NE, Bojan MI, Vedula S, Schanda P, Marx A, Bronstein AM. 2025. Inverse problems with experiment-guided AlphaFold. Proceedings of the 42nd International Conference on Machine Learning. ICML: International Conference on Machine Learning, PMLR, vol. 267, 42366–42393.' mla: Maddipatla, Sai A., et al. “Inverse Problems with Experiment-Guided AlphaFold.” Proceedings of the 42nd International Conference on Machine Learning, vol. 267, ML Research Press, 2025, pp. 42366–93. short: S.A. Maddipatla, N.E. Sellam, M.I. Bojan, S. Vedula, P. Schanda, A. Marx, A.M. Bronstein, in:, Proceedings of the 42nd International Conference on Machine Learning, ML Research Press, 2025, pp. 42366–42393. conference: end_date: 2025-07-19 location: Vancouver, Canada name: 'ICML: International Conference on Machine Learning' start_date: 2025-07-13 corr_author: '1' date_created: 2026-02-18T12:11:17Z date_published: 2025-07-30T00:00:00Z date_updated: 2026-02-19T08:56:43Z day: '30' ddc: - '000' - '540' department: - _id: PaSc - _id: AlBr - _id: GradSch external_id: arxiv: - '2502.09372' file: - access_level: open_access checksum: f33230a6d59b7978d4cd72795e4e9059 content_type: application/pdf creator: dernst date_created: 2026-02-19T08:56:10Z date_updated: 2026-02-19T08:56:10Z file_id: '21338' file_name: 2025_ICML_Maddipatla.pdf file_size: 1924177 relation: main_file success: 1 file_date_updated: 2026-02-19T08:56:10Z has_accepted_license: '1' intvolume: ' 267' language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 42366 - 42393 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery - _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0 grant_number: I06223 name: Structure and mechanism of the mitochondrial MIM insertase publication: Proceedings of the 42nd International Conference on Machine Learning publication_identifier: eissn: - 2640-3498 publication_status: published publisher: ML Research Press quality_controlled: '1' status: public title: Inverse problems with experiment-guided AlphaFold tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: conference user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 267 year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '20664' abstract: - lang: eng text: Conference travel contributes to the climate footprint of academic research. Here, we provide a quantitative estimate of the carbon emissions associated with conference attendance by analyzing travel data from participants of 10 international conferences in the field of magnetic resonance, namely EUROMAR, ENC and ICMRBS. We find that attending a EUROMAR conference produces, on average, more than 1 t CO2 eq.. For the analyzed conferences outside Europe, the corresponding value is about 2–3 times higher, on average, with intercontinental trips amounting to up to 5 t. We compare these conference-related emissions to other activities associated with research and show that conference travel is a substantial portion of the total climate footprint of a researcher in magnetic resonance. We explore several strategies to reduce these emissions, including the impact of selecting conference venues more strategically and the possibility of decentralized conferences. Through a detailed comparison of train versus air travel – accounting for both direct and infrastructure-related emissions – we demonstrate that train travel offers considerable carbon savings. These data may provide a basis for strategic choices of future conferences in the field and for individuals deciding on their conference attendance. acknowledgement: 'First and foremost, we are grateful to the conference organizers who have provided data, either in the form of tables or by pointing us to abstract books. We thank the reviewers and the handling editor (Gottfried Otting) for the careful reading and suggestions. This project emerged from an interactive course about energy and climate, held at IST Austria by Jeroen Dobbelaere, Georgios Katsaros and Paul Schanda. We are grateful to ISTA''s Graduate School for enabling this interdisciplinary course and to all participating students. We thank the following persons for discussions and/or comments about the manuscript: Helene Van Melckebeke, Mei Hong, Jeff Hoch, Gottfried Otting and Matthias Ernst. For the preparation of the manuscript, AI tools have been used, namely for finding relevant literature (ChatGPT) and for correcting the text (Writefull, within Overleaf LaTeX).' article_processing_charge: Yes article_type: original author: - first_name: Lucky full_name: Kapoor, Lucky id: 84b9700b-15b2-11ec-abd3-831089e67615 last_name: Kapoor orcid: 0000-0001-8319-2148 - first_name: Natalia full_name: Ruzickova, Natalia id: D2761128-D73D-11E9-A1BF-BA0DE6697425 last_name: Ruzickova - first_name: Predrag full_name: Zivadinovic, Predrag id: 68AA0E5A-AFDA-11E9-9994-141DE6697425 last_name: Zivadinovic - first_name: Valentin full_name: Leitner, Valentin id: 4c665ce3-0016-11ec-bea0-e44de7a4fa3d last_name: Leitner - first_name: Maria A full_name: Sisak, Maria A id: 44A03D04-AEA4-11E9-B225-EA2DE6697425 last_name: Sisak - first_name: Cecelia N full_name: Mweka, Cecelia N id: 2a69ab4b-896a-11ed-bdf8-cb8641cf2b21 last_name: Mweka - first_name: Jeroen A full_name: Dobbelaere, Jeroen A id: c15a5412-de82-11ed-b809-8dc1aa996e40 last_name: Dobbelaere - first_name: Georgios full_name: Katsaros, Georgios id: 38DB5788-F248-11E8-B48F-1D18A9856A87 last_name: Katsaros orcid: 0000-0001-8342-202X - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Kapoor L, Ruzickova N, Zivadinovic P, et al. Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. 2025;6(2):243-256. doi:10.5194/mr-6-243-2025' apa: 'Kapoor, L., Ruzickova, N., Zivadinovic, P., Leitner, V., Sisak, M. A., Mweka, C. N., … Schanda, P. (2025). Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-6-243-2025' chicago: 'Kapoor, Lucky, Natalia Ruzickova, Predrag Zivadinovic, Valentin Leitner, Maria A Sisak, Cecelia N Mweka, Jeroen A Dobbelaere, Georgios Katsaros, and Paul Schanda. “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” Magnetic Resonance. Copernicus Publications, 2025. https://doi.org/10.5194/mr-6-243-2025.' ieee: 'L. Kapoor et al., “Quantifying the carbon footprint of conference travel: The case of NMR meetings,” Magnetic Resonance, vol. 6, no. 2. Copernicus Publications, pp. 243–256, 2025.' ista: 'Kapoor L, Ruzickova N, Zivadinovic P, Leitner V, Sisak MA, Mweka CN, Dobbelaere JA, Katsaros G, Schanda P. 2025. Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. 6(2), 243–256.' mla: 'Kapoor, Lucky, et al. “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” Magnetic Resonance, vol. 6, no. 2, Copernicus Publications, 2025, pp. 243–56, doi:10.5194/mr-6-243-2025.' short: L. Kapoor, N. Ruzickova, P. Zivadinovic, V. Leitner, M.A. Sisak, C.N. Mweka, J.A. Dobbelaere, G. Katsaros, P. Schanda, Magnetic Resonance 6 (2025) 243–256. corr_author: '1' date_created: 2025-11-23T23:01:39Z date_published: 2025-11-10T00:00:00Z date_updated: 2026-04-28T13:15:31Z day: '10' ddc: - '000' department: - _id: JoFi - _id: GaTk - _id: JoCs - _id: EvBe - _id: TaHa - _id: GradSch - _id: GeKa - _id: PaSc doi: 10.5194/mr-6-243-2025 file: - access_level: open_access checksum: c63dd47b0e77f9451821436bb77d27c9 content_type: application/pdf creator: dernst date_created: 2025-11-24T08:25:19Z date_updated: 2025-11-24T08:25:19Z file_id: '20672' file_name: 2025_MagneticResonance_Kapoor.pdf file_size: 3081399 relation: main_file success: 1 file_date_updated: 2025-11-24T08:25:19Z has_accepted_license: '1' intvolume: ' 6' issue: '2' language: - iso: eng month: '11' oa: 1 oa_version: Published Version page: 243-256 publication: Magnetic Resonance publication_identifier: eissn: - 2699-0016 publication_status: published publisher: Copernicus Publications quality_controlled: '1' related_material: link: - description: News on ISTA website relation: research_data url: https://ista.ac.at/en/news/carbon-footprint-of-conference-travel/ record: - id: '20242' relation: research_data status: public scopus_import: '1' status: public title: 'Quantifying the carbon footprint of conference travel: The case of NMR meetings' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd volume: 6 year: '2025' ... --- _id: '20242' abstract: - lang: eng text: "This repository contains calculations of carbon footprints of NMR conferences, as described in the article by \r\nLucky N. Kapoor, Natalia Ruzickova, Predrag Živadinović, Valentin Leitner, Maria Anna Sisak, Cecelia Mweka, Jeroen Dobbelaere, Georgios Katsaros, and Paul Schanda\r\nPublished in Magnetic Resonance, 2025." article_processing_charge: No author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Schanda P. Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” 2025. doi:10.15479/AT-ISTA-20242' apa: 'Schanda, P. (2025). Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20242' chicago: 'Schanda, Paul. “Data of: ‘Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20242.' ieee: 'P. Schanda, “Data of: ‘Quantifying the carbon footprint of conference travel: the case of NMR meetings.’” Institute of Science and Technology Austria, 2025.' ista: 'Schanda P. 2025. Data of: ‘Quantifying the carbon footprint of conference travel: the case of NMR meetings’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-20242.' mla: 'Schanda, Paul. Data of: “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-20242.' short: P. Schanda, (2025). contributor: - contributor_type: researcher first_name: Natalia id: D2761128-D73D-11E9-A1BF-BA0DE6697425 last_name: Ruzickova - contributor_type: researcher first_name: Lucky id: 84b9700b-15b2-11ec-abd3-831089e67615 last_name: Kapoor - contributor_type: researcher first_name: Valentin id: 4c665ce3-0016-11ec-bea0-e44de7a4fa3d last_name: Leitner - contributor_type: researcher first_name: Predrag id: 68AA0E5A-AFDA-11E9-9994-141DE6697425 last_name: Zivadinovic - contributor_type: researcher first_name: Maria A id: 44A03D04-AEA4-11E9-B225-EA2DE6697425 last_name: Sisak - contributor_type: researcher first_name: Cecelia N id: 2a69ab4b-896a-11ed-bdf8-cb8641cf2b21 last_name: Mweka - contributor_type: supervisor first_name: Jeroen A id: c15a5412-de82-11ed-b809-8dc1aa996e40 last_name: Dobbelaere - contributor_type: supervisor first_name: Georgios id: 38DB5788-F248-11E8-B48F-1D18A9856A87 last_name: Katsaros orcid: 0000-0001-8342-202X corr_author: '1' date_created: 2025-08-31T15:14:18Z date_published: 2025-09-01T00:00:00Z date_updated: 2026-04-28T13:15:30Z department: - _id: PaSc doi: 10.15479/AT-ISTA-20242 file: - access_level: open_access checksum: 055044b03f835cb98c45d0504f1db96e content_type: application/zip creator: pschanda date_created: 2025-08-31T15:09:44Z date_updated: 2025-08-31T15:09:44Z file_id: '20244' file_name: Abstracts.zip file_size: 42368943 relation: main_file success: 1 - access_level: open_access checksum: 1492683af736ac65088b77e12b52c3b0 content_type: application/zip creator: pschanda date_created: 2025-08-31T15:11:58Z date_updated: 2025-08-31T15:11:58Z file_id: '20245' file_name: data_CO2_conferences.zip file_size: 470659 relation: main_file success: 1 - access_level: open_access checksum: 8ac69071f7508e77b5ca91fa5018339a content_type: application/zip creator: pschanda date_created: 2025-08-31T15:12:03Z date_updated: 2025-08-31T15:12:03Z file_id: '20246' file_name: Figure6_predictions.zip file_size: 1138772 relation: main_file success: 1 - access_level: open_access checksum: 19b77db247feecdc36fbe6f68d94a76d content_type: text/x-python-script creator: pschanda date_created: 2025-08-31T15:12:07Z date_updated: 2025-08-31T15:12:07Z file_id: '20247' file_name: ExcelFileAnalysisCode.py file_size: 6558 relation: main_file success: 1 - access_level: open_access checksum: 39655e28c6df523f4f9662dc58c94623 content_type: application/pdf creator: pschanda date_created: 2025-08-31T15:12:11Z date_updated: 2025-08-31T15:12:11Z file_id: '20248' file_name: emissions_spectrometers_and_Parisgoal.pdf file_size: 1107467 relation: main_file success: 1 - access_level: open_access checksum: 2e9a9460b3f2abe7e46179561a63492b content_type: application/octet-stream creator: pschanda date_created: 2025-09-01T11:05:27Z date_updated: 2025-09-01T11:05:27Z file_id: '20263' file_name: README file_size: 3994 relation: main_file success: 1 file_date_updated: 2025-09-01T11:05:27Z has_accepted_license: '1' keyword: - sustainability - conference travel month: '09' oa: 1 oa_version: None publisher: Institute of Science and Technology Austria related_material: record: - id: '20664' relation: used_in_publication status: public status: public title: 'Data of: "Quantifying the carbon footprint of conference travel: the case of NMR meetings"' tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2025' ... --- OA_type: closed access _id: '18167' abstract: - lang: eng text: 'Holdase chaperones are essential in the mitochondrial membrane-protein biogenesis as they stabilize preproteins and keep them in an import-competent state as they travel through the aqueous cytosol and intermembrane space. The small TIM chaperones of the mitochondrial intermembrane space function within a fine balance of client promiscuity and high affinity binding, while being also able to release their client proteins without significant energy barrier to the downstream insertases/translocases. The tendency of the preproteins to aggregate and the dynamic nature of the preprotein—chaperone complexes makes the preparation of these complexes challenging. Here we present two optimized methods for complex formation of highly hydrophobic precursor proteins and chaperones: a pull-down approach and an in-vitro translation strategy. In the former, attaching the client protein to an affinity resin keeps the individual client protein copies apart from each other and decreases the client self-aggregation probability, thereby favouring complex formation. In the latter approach, a purified chaperone, added to the cell-free protein synthesis, captures the nascent precursor protein. The choice of method will depend on the desired client-chaperone complex amount, or the need for specific labeling scheme.' article_processing_charge: No author: - first_name: Undina full_name: Guillerm, Undina id: bb74f472-ae54-11eb-9835-bc9c22fb1183 last_name: Guillerm - first_name: Iva full_name: Sučec, Iva last_name: Sučec - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Guillerm U, Sučec I, Schanda P. Generation of TIM chaperone substrate complexes. In: Methods in Enzymology. Vol 707. Elsevier; 2024:391-422. doi:10.1016/bs.mie.2024.07.051' apa: Guillerm, U., Sučec, I., & Schanda, P. (2024). Generation of TIM chaperone substrate complexes. In Methods in Enzymology (Vol. 707, pp. 391–422). Elsevier. https://doi.org/10.1016/bs.mie.2024.07.051 chicago: Guillerm, Undina, Iva Sučec, and Paul Schanda. “Generation of TIM Chaperone Substrate Complexes.” In Methods in Enzymology, 707:391–422. Elsevier, 2024. https://doi.org/10.1016/bs.mie.2024.07.051. ieee: U. Guillerm, I. Sučec, and P. Schanda, “Generation of TIM chaperone substrate complexes,” in Methods in Enzymology, vol. 707, Elsevier, 2024, pp. 391–422. ista: 'Guillerm U, Sučec I, Schanda P. 2024.Generation of TIM chaperone substrate complexes. In: Methods in Enzymology. vol. 707, 391–422.' mla: Guillerm, Undina, et al. “Generation of TIM Chaperone Substrate Complexes.” Methods in Enzymology, vol. 707, Elsevier, 2024, pp. 391–422, doi:10.1016/bs.mie.2024.07.051. short: U. Guillerm, I. Sučec, P. Schanda, in:, Methods in Enzymology, Elsevier, 2024, pp. 391–422. corr_author: '1' date_created: 2024-10-01T10:58:27Z date_published: 2024-09-13T00:00:00Z date_updated: 2025-10-22T06:40:54Z day: '13' department: - _id: PaSc doi: 10.1016/bs.mie.2024.07.051 external_id: pmid: - '39488384' intvolume: ' 707' language: - iso: eng month: '09' oa_version: None page: 391-422 pmid: 1 publication: Methods in Enzymology publication_identifier: issn: - 0076-6879 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Generation of TIM chaperone substrate complexes type: book_chapter user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 707 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '18910' abstract: - lang: eng text: Proteins often undergo large-scale conformational transitions, in which secondary and tertiary structure elements (loops, helices, and domains) change their structures or their positions with respect to each other. Simple considerations suggest that such dynamics should be relatively fast, but the functional cycles of many proteins are often relatively slow. Sophisticated experimental methods are starting to tackle this dichotomy and shed light on the contribution of large-scale conformational dynamics to protein function. In this review, we focus on the contribution of single-molecule Förster resonance energy transfer and nuclear magnetic resonance (NMR) spectroscopies to the study of conformational dynamics. We briefly describe the state of the art in each of these techniques and then point out their similarities and differences, as well as the relative strengths and weaknesses of each. Several case studies, in which the connection between fast conformational dynamics and slower function has been demonstrated, are then introduced and discussed. These examples include both enzymes and large protein machines, some of which have been studied by both NMR and fluorescence spectroscopies. acknowledgement: G.H. is the incumbent of the Hilda Pomeraniec Memorial Professorial Chair. He has been partially funded by the European Research Council under the European Union's Horizon 2020 research and innovation program (grant 742637, SMALLOSTERY), by National Science Foundation–US-Israel Binational Science Foundation grant 2021700, and by an Israel Science Foundation Breakthrough grant (1924/22). P.S. acknowledges funding from the Austrian Science Fund (project “AlloSpace,” I05812) and intramural funding from the Institute of Science and Technology Austria. article_processing_charge: No article_type: original author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Gilad full_name: Haran, Gilad last_name: Haran citation: ama: Schanda P, Haran G. NMR and single-molecule FRET insights into fast protein motions and their relation to function. Annual Review of Biophysics. 2024;53:247-273. doi:10.1146/annurev-biophys-070323-022428 apa: Schanda, P., & Haran, G. (2024). NMR and single-molecule FRET insights into fast protein motions and their relation to function. Annual Review of Biophysics. Annual Reviews. https://doi.org/10.1146/annurev-biophys-070323-022428 chicago: Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” Annual Review of Biophysics. Annual Reviews, 2024. https://doi.org/10.1146/annurev-biophys-070323-022428. ieee: P. Schanda and G. Haran, “NMR and single-molecule FRET insights into fast protein motions and their relation to function,” Annual Review of Biophysics, vol. 53. Annual Reviews, pp. 247–273, 2024. ista: Schanda P, Haran G. 2024. NMR and single-molecule FRET insights into fast protein motions and their relation to function. Annual Review of Biophysics. 53, 247–273. mla: Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” Annual Review of Biophysics, vol. 53, Annual Reviews, 2024, pp. 247–73, doi:10.1146/annurev-biophys-070323-022428. short: P. Schanda, G. Haran, Annual Review of Biophysics 53 (2024) 247–273. corr_author: '1' date_created: 2025-01-27T13:40:34Z date_published: 2024-07-01T00:00:00Z date_updated: 2025-09-09T12:06:24Z day: '01' ddc: - '570' department: - _id: PaSc doi: 10.1146/annurev-biophys-070323-022428 external_id: isi: - '001278237500012' pmid: - '38346243' file: - access_level: open_access checksum: c90861542ae3f9147939030d5bafed3c content_type: application/pdf creator: dernst date_created: 2025-01-27T13:44:59Z date_updated: 2025-01-27T13:44:59Z file_id: '18911' file_name: 2024_AnnualReviews_Schanda.pdf file_size: 3025589 relation: main_file success: 1 file_date_updated: 2025-01-27T13:44:59Z has_accepted_license: '1' intvolume: ' 53' isi: 1 language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 247-273 pmid: 1 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Annual Review of Biophysics publication_identifier: eissn: - 1936-1238 issn: - 1936-122X publication_status: published publisher: Annual Reviews quality_controlled: '1' scopus_import: '1' status: public title: NMR and single-molecule FRET insights into fast protein motions and their relation to function tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 53 year: '2024' ... --- _id: '17042' abstract: - lang: eng text: 'Bacterial cell walls are gigadalton-large cross-linked polymers with a wide range of motional amplitudes, including rather rigid as well as highly flexible parts. Magic-angle spinning NMR is a powerful method to obtain atomic-level information about intact cell walls. Here we investigate sensitivity and information content of different homonuclear 13C-13C and heteronuclear H-N, H-C and N-C correlation experiments. We demonstrate that a CPMAS CryoProbe yields ca. 8-fold increased signal-to-noise over a room-temperature probe, or a ca. 3-4-fold larger per-mass sensitivity. The increased sensitivity allowed to obtain high-resolution spectra even on intact bacteria. Moreover, we compare resolution and sensitivity of 1H MAS experiments obtained at 100 kHz vs. 55 kHz. Our study provides useful hints for choosing experiments to extract atomic-level details on cell-wall samples. ' article_processing_charge: No author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Schanda P. Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” 2024. doi:10.15479/AT:ISTA:17042' apa: 'Schanda, P. (2024). Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:17042' chicago: 'Schanda, Paul. “Raw Data to ‘MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.’” Institute of Science and Technology Austria, 2024. https://doi.org/10.15479/AT:ISTA:17042.' ieee: 'P. Schanda, “Raw data to ‘MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.’” Institute of Science and Technology Austria, 2024.' ista: 'Schanda P. 2024. Raw data to ‘MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments’, Institute of Science and Technology Austria, 10.15479/AT:ISTA:17042.' mla: 'Schanda, Paul. Raw Data to “MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.” Institute of Science and Technology Austria, 2024, doi:10.15479/AT:ISTA:17042.' short: P. Schanda, (2024). contributor: - contributor_type: data_collector first_name: Alicia last_name: Vallet - contributor_type: data_collector first_name: 'Isabel ' last_name: Ayala - contributor_type: data_collector first_name: Barbara last_name: Perrone - contributor_type: data_collector first_name: Alia last_name: Hassan - contributor_type: data_collector first_name: Catherine last_name: Bougault corr_author: '1' date_created: 2024-05-22T12:04:54Z date_published: 2024-05-22T00:00:00Z date_updated: 2025-09-09T12:01:41Z day: '22' ddc: - '570' department: - _id: PaSc doi: 10.15479/AT:ISTA:17042 file: - access_level: open_access checksum: eb55f0988342d927702353b75e07edfa content_type: text/plain creator: pschanda date_created: 2024-05-22T12:05:13Z date_updated: 2024-05-22T12:05:13Z file_id: '17043' file_name: Read_me.txt file_size: 2132 relation: main_file success: 1 - access_level: open_access checksum: 3393592acaf5ee1e032052c236780914 content_type: application/zip creator: pschanda date_created: 2024-05-22T12:17:10Z date_updated: 2024-05-22T12:17:10Z file_id: '17044' file_name: raw_data_CryoMAS_cyronebacteria.zip file_size: 755704888 relation: main_file success: 1 file_date_updated: 2024-05-22T12:17:10Z has_accepted_license: '1' keyword: - nuclear magnetic resonance - NMR - cellwall - structural biology - spectroscopy month: '05' oa: 1 oa_version: Published Version publisher: Institute of Science and Technology Austria related_material: record: - id: '17291' relation: used_in_publication status: public status: public title: 'Raw data to "MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments"' tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: research_data user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2024' ... --- _id: '17161' abstract: - lang: eng text: Dynamic processes in molecules can occur on a wide range of timescales, and it is important to understand which timescales of motion contribute to different parameters used in dynamics measurements. For spin relaxation, this can easily be understood from the sampling frequencies of the spectral-density function by different relaxation-rate constants. In addition to data from relaxation measurements, determining dynamically averaged anisotropic interactions in magic-angle spinning (MAS) solid-state NMR allows for better quantification of the amplitude of molecular motion. For partially averaged anisotropic interactions, the relevant timescales of motion are not so clearly defined. Whether the averaging depends on the experimental methods (e.g., pulse sequences) or conditions (e.g., MAS frequency, magnitude of anisotropic interaction, radio-frequency field amplitudes) is not fully understood. To investigate these questions, we performed numerical simulations of dynamic systems based on the stochastic Liouville equation using several experiments for recoupling the dipolar coupling, chemical-shift anisotropy or quadrupolar coupling. As described in the literature, the transition between slow motion, where parameters characterizing the anisotropic interaction are not averaged, and fast motion, where the tensors are averaged leading to a scaled anisotropic quantity, occurs over a window of motional rate constants that depends mainly on the strength of the interaction. This transition region can span 2 orders of magnitude in exchange-rate constants (typically in the microsecond range) but depends only marginally on the employed recoupling scheme or sample spinning frequency. The transition region often coincides with a fast relaxation of coherences, making precise quantitative measurements difficult. Residual couplings in off-magic-angle experiments, however, average over longer timescales of motion. While in principle one may gain information on the timescales of motion from the transition area, extracting such information is hampered by low signal-to-noise ratio in experimental spectra due to fast relaxation that occurs in the same region. acknowledgement: "We would like to thank Kay Saalwächter for pointing out important aspects of the intermediate regime during the open review process. Lea Marie Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria.\r\nThis research has been supported by the Österreichischen Akademie der Wissenschaften (grant no. PR10660EAW01) and the Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (grant nos. 200020_188988 and 200020_219375)." article_processing_charge: Yes article_type: original author: - first_name: Kathrin full_name: Aebischer, Kathrin last_name: Aebischer - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Matthias full_name: Ernst, Matthias last_name: Ernst citation: ama: Aebischer K, Becker LM, Schanda P, Ernst M. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic Resonance. 2024;5(1):69-86. doi:10.5194/mr-5-69-2024 apa: Aebischer, K., Becker, L. M., Schanda, P., & Ernst, M. (2024). Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-5-69-2024 chicago: Aebischer, Kathrin, Lea Marie Becker, Paul Schanda, and Matthias Ernst. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” Magnetic Resonance. Copernicus Publications, 2024. https://doi.org/10.5194/mr-5-69-2024. ieee: K. Aebischer, L. M. Becker, P. Schanda, and M. Ernst, “Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR,” Magnetic Resonance, vol. 5, no. 1. Copernicus Publications, pp. 69–86, 2024. ista: Aebischer K, Becker LM, Schanda P, Ernst M. 2024. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic Resonance. 5(1), 69–86. mla: Aebischer, Kathrin, et al. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” Magnetic Resonance, vol. 5, no. 1, Copernicus Publications, 2024, pp. 69–86, doi:10.5194/mr-5-69-2024. short: K. Aebischer, L.M. Becker, P. Schanda, M. Ernst, Magnetic Resonance 5 (2024) 69–86. date_created: 2024-06-23T22:01:02Z date_published: 2024-06-11T00:00:00Z date_updated: 2025-06-11T13:26:12Z day: '11' ddc: - '530' department: - _id: PaSc doi: 10.5194/mr-5-69-2024 external_id: pmid: - '40384772' file: - access_level: open_access checksum: d01074f6919387fcaf8c9ebed320ccae content_type: application/pdf creator: dernst date_created: 2024-06-27T06:42:55Z date_updated: 2024-06-27T06:42:55Z file_id: '17181' file_name: 2024_MagneticResonance_Aebischer.pdf file_size: 6736194 relation: main_file success: 1 file_date_updated: 2024-06-27T06:42:55Z has_accepted_license: '1' intvolume: ' 5' issue: '1' language: - iso: eng month: '06' oa: 1 oa_version: Published Version page: 69-86 pmid: 1 project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publication: Magnetic Resonance publication_identifier: eissn: - 2699-0016 publication_status: published publisher: Copernicus Publications quality_controlled: '1' scopus_import: '1' status: public title: Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 5 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '17291' abstract: - lang: eng text: Bacterial cell walls are gigadalton-large cross-linked polymers with a wide range of motional amplitudes, including rather rigid as well as highly flexible parts. Magic-angle spinning NMR is a powerful method to obtain atomic-level information about intact cell walls. Here we investigate sensitivity and information content of different homonuclear 13Csingle bond13C and heteronuclear 1Hsingle bond15N, 1Hsingle bond13C and 15Nsingle bond13C correlation experiments. We demonstrate that a CPMAS CryoProbe yields ca. 8-fold increased signal-to-noise over a room-temperature probe, or a ca. 3–4-fold larger per-mass sensitivity. The increased sensitivity allowed to obtain high-resolution spectra even on intact bacteria. Moreover, we compare resolution and sensitivity of 1H MAS experiments obtained at 100 kHz vs. 55 kHz. Our study provides useful hints for choosing experiments to extract atomic-level details on cell-wall samples. acknowledgement: "This research was supported by the French Agence Nationale de la Recherche (\r\nANR-16-CE11-0030-12, TransPepNMR). This work used the platforms of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI, France (ANR-10-INBS-0005-02\r\n) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche), CBH-EUR-GS (ANR-17-EURE-0003). Financial support from the IR INFRANALYTICS FR2054 for conducting the research and intramural funding by the Institute of Science and Technology Austria (ISTA) are gratefully acknowledged." article_number: '107708' article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Alicia full_name: Vallet, Alicia last_name: Vallet - first_name: Isabel full_name: Ayala, Isabel last_name: Ayala - first_name: Barbara full_name: Perrone, Barbara last_name: Perrone - first_name: Alia full_name: Hassan, Alia last_name: Hassan - first_name: Jean-Pierre full_name: Simorre, Jean-Pierre last_name: Simorre - first_name: Catherine full_name: Bougault, Catherine last_name: Bougault - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Vallet A, Ayala I, Perrone B, et al. MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments. Journal of Magnetic Resonance. 2024;364. doi:10.1016/j.jmr.2024.107708' apa: 'Vallet, A., Ayala, I., Perrone, B., Hassan, A., Simorre, J.-P., Bougault, C., & Schanda, P. (2024). MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2024.107708' chicago: 'Vallet, Alicia, Isabel Ayala, Barbara Perrone, Alia Hassan, Jean-Pierre Simorre, Catherine Bougault, and Paul Schanda. “MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.” Journal of Magnetic Resonance. Elsevier, 2024. https://doi.org/10.1016/j.jmr.2024.107708.' ieee: 'A. Vallet et al., “MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments,” Journal of Magnetic Resonance, vol. 364. Elsevier, 2024.' ista: 'Vallet A, Ayala I, Perrone B, Hassan A, Simorre J-P, Bougault C, Schanda P. 2024. MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments. Journal of Magnetic Resonance. 364, 107708.' mla: 'Vallet, Alicia, et al. “MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.” Journal of Magnetic Resonance, vol. 364, 107708, Elsevier, 2024, doi:10.1016/j.jmr.2024.107708.' short: A. Vallet, I. Ayala, B. Perrone, A. Hassan, J.-P. Simorre, C. Bougault, P. Schanda, Journal of Magnetic Resonance 364 (2024). corr_author: '1' date_created: 2024-07-22T07:44:10Z date_published: 2024-07-01T00:00:00Z date_updated: 2025-09-09T12:01:41Z day: '01' ddc: - '570' department: - _id: PaSc doi: 10.1016/j.jmr.2024.107708 external_id: isi: - '001259302800001' pmid: - '38901173' file: - access_level: open_access checksum: 4b59f4f0c287ecbafd808da1212ced38 content_type: application/pdf creator: dernst date_created: 2024-07-23T06:23:51Z date_updated: 2024-07-23T06:23:51Z file_id: '17316' file_name: 2024_JourMagneticResonance_Vallet.pdf file_size: 2236665 relation: main_file success: 1 file_date_updated: 2024-07-23T06:23:51Z has_accepted_license: '1' intvolume: ' 364' isi: 1 language: - iso: eng month: '07' oa: 1 oa_version: Published Version pmid: 1 publication: Journal of Magnetic Resonance publication_identifier: issn: - 1090-7807 publication_status: published publisher: Elsevier quality_controlled: '1' related_material: record: - id: '17042' relation: research_data status: public scopus_import: '1' status: public title: 'MAS NMR experiments of corynebacterial cell walls: Complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 364 year: '2024' ... --- APC_amount: 1530 EUR OA_place: publisher OA_type: gold _id: '15401' abstract: - lang: eng text: Amide-proton-detected magic-angle-spinning NMR of deuterated proteins has become a main technique in NMR-based structural biology. In standard deuteration protocols that rely on D2O-based culture media, non-exchangeable amide sites remain deuterated, making these sites unobservable. Here we demonstrate that proteins produced with a H2O-based culture medium doped with deuterated cell lysate allow scientists to overcome this “reprotonation bottleneck” while retaining a high level of deuteration (ca. 80 %) and narrow linewidths. We quantified coherence lifetimes of several proteins prepared with this labeling pattern over a range of magic-angle-spinning (MAS) frequencies (40–100 kHz). We demonstrate that under commonly used conditions (50–60 kHz MAS), the amide 1H linewidths with our labeling approach are comparable to those of perdeuterated proteins and better than those of protonated samples at 100 kHz. For three proteins in the 33–50 kDa size range, many previously unobserved amides become visible. We report how to prepare the deuterated cell lysate for our approach from fractions of perdeuterated cultures which are usually discarded, and we show that such media can be used identically to commercial media. The residual protonation of Hα sites allows for well-resolved Hα-detected spectra and Hα resonance assignment, exemplified by the de novo assignment of 168 Hα sites in a 39 kDa protein. The approach based on this H2O/cell-lysate deuteration and MAS frequencies compatible with 1.3 or 1.9 mm rotors presents a strong sensitivity benefit over 0.7 mm 100 kHz MAS experiments. acknowledged_ssus: - _id: NMR acknowledgement: "We thank Dominique Madern (IBS Grenoble) for providing the plasmid for MalDH and feedback on the article, Alicia Vallet for excellent support at the Grenoble NMR facility, and Petra Rovo and Margarita Valhondo at the IST Austria NMR Service Unit. We thank Dorothea Anrather in the mass spectrometry facility of Max Perutz Labs for the mass spectrometry analysis using the instruments of the Vienna BioCenter Core Facilities (VBCF). We are grateful to Jean-Pierre Andrieu (Plateforme Seq3A, IBS Grenoble) for the analysis of the amino acid composition of the in-house-prepared lysates. We are grateful to Rasmus Linser (Technical University Dortmund) for sharing a paper draft describing a similar study. This work was supported by the Austrian Science Fund (FWF; project number I5812-B). We thank Tobias Schubeis (Lyon) and the reviewers for constructive input.\r\nThis research has been supported by the Austrian Science Fund (grant no. I5812-B). Part of this work used the platforms of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for 40 Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). IBS acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, 45 CEA). Charles-Adrien Arnaud was funded by GRAL." article_processing_charge: Yes article_type: original author: - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - first_name: Jia-Ying full_name: Guan, Jia-Ying last_name: Guan - first_name: Charles-Adrien full_name: Arnaud, Charles-Adrien last_name: Arnaud - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Hugo full_name: Fraga, Hugo last_name: Fraga - first_name: Cécile full_name: Breyton, Cécile last_name: Breyton - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Napoli F, Guan J-Y, Arnaud C-A, et al. Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic Resonance. 2024;5(1):33-49. doi:10.5194/mr-5-33-2024' apa: 'Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C., & Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-5-33-2024' chicago: 'Napoli, Federico, Jia-Ying Guan, Charles-Adrien Arnaud, Pavel Macek, Hugo Fraga, Cécile Breyton, and Paul Schanda. “Deuteration of Proteins Boosted by Cell Lysates: High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the Reprotonation Bottleneck.” Magnetic Resonance. Copernicus Publications, 2024. https://doi.org/10.5194/mr-5-33-2024.' ieee: 'F. Napoli et al., “Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck,” Magnetic Resonance, vol. 5, no. 1. Copernicus Publications, pp. 33–49, 2024.' ista: 'Napoli F, Guan J-Y, Arnaud C-A, Macek P, Fraga H, Breyton C, Schanda P. 2024. Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic Resonance. 5(1), 33–49.' mla: 'Napoli, Federico, et al. “Deuteration of Proteins Boosted by Cell Lysates: High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the Reprotonation Bottleneck.” Magnetic Resonance, vol. 5, no. 1, Copernicus Publications, 2024, pp. 33–49, doi:10.5194/mr-5-33-2024.' short: F. Napoli, J.-Y. Guan, C.-A. Arnaud, P. Macek, H. Fraga, C. Breyton, P. Schanda, Magnetic Resonance 5 (2024) 33–49. corr_author: '1' date_created: 2024-05-16T15:02:43Z date_published: 2024-04-19T00:00:00Z date_updated: 2025-07-17T08:12:23Z day: '19' ddc: - '530' department: - _id: PaSc doi: 10.5194/mr-5-33-2024 external_id: pmid: - '40384771' file: - access_level: open_access checksum: 80ea50114e428461ca9530d3bd5d89e4 content_type: application/pdf creator: dernst date_created: 2024-05-22T07:01:15Z date_updated: 2024-05-22T07:01:15Z file_id: '15413' file_name: 2024_MagneticResonance_Napoli.pdf file_size: 6657865 relation: main_file success: 1 file_date_updated: 2024-05-22T07:01:15Z has_accepted_license: '1' intvolume: ' 5' issue: '1' language: - iso: eng month: '04' oa: 1 oa_version: Published Version page: 33-49 pmid: 1 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery - _id: 3AC91DDA-15DF-11EA-824D-93A3E7B544D1 call_identifier: FWF name: FWF Open Access Fund publication: Magnetic Resonance publication_identifier: issn: - 2699-0016 publication_status: published publisher: Copernicus Publications quality_controlled: '1' scopus_import: '1' status: public title: 'Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 5 year: '2024' ...