[{"year":"2026","ddc":["540"],"project":[{"name":"IST Austria Open Access Fund","_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854"},{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777"}],"publisher":"Copernicus Publications","page":"29-37","article_processing_charge":"Yes","date_published":"2026-04-16T00:00:00Z","pmid":1,"volume":7,"intvolume":"         7","author":[{"orcid":"0000-0002-6401-5151","first_name":"Lea Marie","last_name":"Becker","full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"last_name":"Toscano","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","full_name":"Toscano, Giorgia","first_name":"Giorgia"},{"first_name":"Anna","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna"},{"first_name":"Rajkumar","last_name":"Singh","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20","full_name":"Singh, Rajkumar"},{"first_name":"Undina","last_name":"Guillerm","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","full_name":"Guillerm, Undina"},{"last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J.","first_name":"Roman J."},{"first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda"}],"_id":"21777","issue":"1","external_id":{"pmid":["42057802"]},"scopus_import":"1","acknowledgement":"We thank Ben P. Tatman for insightful discussions. This research was supported by the Scientific Service Units (SSUs) of ISTA through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. We thank Prof. Tobias Madl (Medical University Graz) for a sample of Omniscan. Lea M. Becker is the recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01).","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"citation":{"ieee":"L. M. Becker <i>et al.</i>, “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants,” <i>Magnetic Resonance</i>, vol. 7, no. 1. Copernicus Publications, pp. 29–37, 2026.","ama":"Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. 2026;7(1):29-37. doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>","apa":"Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker, R. J., &#38; Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>","chicago":"Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>. Copernicus Publications, 2026. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>.","mla":"Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>, vol. 7, no. 1, Copernicus Publications, 2026, pp. 29–37, doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>.","short":"L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37.","ista":"Becker LM, Toscano G, Kapitonova A, Singh R, Guillerm U, Lichtenecker RJ, Schanda P. 2026. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. Magnetic Resonance. 7(1), 29–37."},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.5194/mr-7-29-2026"}],"status":"public","quality_controlled":"1","oa_version":"Published Version","language":[{"iso":"eng"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publication_status":"published","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"doi":"10.5194/mr-7-29-2026","day":"16","month":"04","corr_author":"1","DOAJ_listed":"1","type":"journal_article","date_updated":"2026-05-07T06:49:59Z","PlanS_conform":"1","date_created":"2026-05-03T22:01:36Z","publication":"Magnetic Resonance","publication_identifier":{"eissn":["2699-0016"]},"abstract":[{"lang":"eng","text":"The advantageous characteristics attributed to the 19F nucleus have made it a popular target for nuclear magnetic resonance (NMR) once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilised 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-labelled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labelled 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 TET2 using a mutagenesis approach."}],"has_accepted_license":"1","oa":1,"title":"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","OA_type":"gold","article_type":"original","OA_place":"publisher"},{"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 labelling 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 crystal structure of a GB1 variant reported in this work, reproduce these elevated barriers and reveal how the crystal restrains motions."}],"publication_identifier":{"issn":["17554330"],"eissn":["17554349"]},"date_created":"2026-06-21T22:03:01Z","publication":"Nature Chemistry","PlanS_conform":"1","date_updated":"2026-06-24T08:47:58Z","type":"journal_article","OA_place":"publisher","article_type":"original","OA_type":"hybrid","title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","researchdata_availability":"yes","oa":1,"has_accepted_license":"1","das_tickbox":"1","main_file_link":[{"url":"https://doi.org/10.1038/s41557-026-02155-0","open_access":"1"}],"status":"public","citation":{"short":"L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry (2026).","mla":"Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>.","chicago":"Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot, and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>.","ista":"Becker LM, Fu H, Tatman B, Dreydoppel M, Kapitonova A, Balazs D, Weininger U, Engilberge S, Chipot C, Schanda P. 2026. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. Nature Chemistry.","ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>. Springer Nature, 2026.","ama":"Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>","apa":"Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs, D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>"},"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"scopus_import":"1","acknowledgement":"We thank N. R. Skrynnikov and O. O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to T. Schubeis (Lyon) for advice on GB1 crystallization and R. Schmid for initial crystallization trials. We thank C. Mueller-Dieckmann for assistance with room-temperature X-ray crystallography data collection on beamline ID30B at the ESRF, which is acknowledged for providing beamtime through its In-House Research programme. We thank S. Falkner for assistance with constructing the structural model of the IgG:GB1 complex. We thank J. Lewandowski for providing feedback on the paper and granting access to backbone relaxation data of IgG:GB1T2Q and GB1T2Q microcrystals. This research was supported by the Scientific Service Units (SSU) of the Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank P. Rovó and M. V. Falcón for excellent support of the NMR facility. L.M.B. is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant number PR10660EAW01). C.C. 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.Open access funding provided by Institute of Science and Technology (IST Austria).","corr_author":"1","month":"06","related_material":{"record":[{"status":"public","id":"20641","relation":"research_data"},{"status":"public","id":"21145","relation":"research_data"}]},"day":"10","doi":"10.1038/s41557-026-02155-0","publication_status":"epub_ahead","department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"language":[{"iso":"eng"}],"quality_controlled":"1","oa_version":"Published Version","_id":"22105","external_id":{"pmid":["42271006"]},"author":[{"full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","last_name":"Becker","orcid":"0000-0002-6401-5151","first_name":"Lea Marie"},{"first_name":"Haohao","full_name":"Fu, Haohao","last_name":"Fu"},{"first_name":"Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin"},{"first_name":"Matthias","full_name":"Dreydoppel, Matthias","last_name":"Dreydoppel"},{"first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna","last_name":"Kapitonova"},{"first_name":"Daniel","orcid":"0000-0001-7597-043X","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","full_name":"Balazs, Daniel","last_name":"Balazs"},{"last_name":"Weininger","full_name":"Weininger, Ulrich","first_name":"Ulrich"},{"first_name":"Sylvain","last_name":"Engilberge","full_name":"Engilberge, Sylvain"},{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"dataavailabilitystatement":"The cryo and room-temperature crystal structures of GB1QDD are deposited at the PDB under the access codes 9I2I and 9T8Z, respectively. The solid-state NMR backbone assignment of GB1QDD is deposited at the BMRB under the access code 53330. NMR spectra, analysis scripts and raw data are publicly available at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-20641)120. Files to reproduce the enhanced-sampling MD simulations are publicly available at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-21145)121.","supplementarymaterial":"yes","publisher":"Springer Nature","project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"ddc":["540"],"year":"2026","date_published":"2026-06-10T00:00:00Z","pmid":1,"article_processing_charge":"Yes (via OA deal)"},{"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"oa_version":"Published Version","quality_controlled":"1","language":[{"iso":"eng"}],"corr_author":"1","month":"12","related_material":{"record":[{"id":"19956","relation":"research_data","status":"public"}]},"day":"01","doi":"10.1016/j.jmb.2025.169379","publication_status":"published","department":[{"_id":"PaSc"}],"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.","scopus_import":"1","status":"public","citation":{"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.","short":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda, Journal of Molecular Biology 437 (2025).","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.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>.","mla":"Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>.","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. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>","apa":"Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38; Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>","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,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025."},"file":[{"file_name":"2025_JourMolecularBiology_Rohden.pdf","date_created":"2025-12-29T14:51:40Z","file_id":"20876","creator":"dernst","file_size":2270555,"date_updated":"2025-12-29T14:51:40Z","access_level":"open_access","success":1,"checksum":"90d50594d8ea9860ac5da41297992847","relation":"main_file","content_type":"application/pdf"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"oa":1,"has_accepted_license":"1","OA_place":"publisher","article_type":"original","OA_type":"hybrid","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme","file_date_updated":"2025-12-29T14:51:40Z","PlanS_conform":"1","date_updated":"2026-06-10T08:20:37Z","type":"journal_article","abstract":[{"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.","lang":"eng"}],"publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"date_created":"2025-08-31T22:01:33Z","publication":"Journal of Molecular Biology","article_processing_charge":"Yes (via OA deal)","date_published":"2025-12-01T00:00:00Z","article_number":"169379","year":"2025","publisher":"Elsevier","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"ddc":["540"],"author":[{"first_name":"Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","full_name":"Rohden, Darja","last_name":"Rohden"},{"orcid":"0000-0002-9043-136X","first_name":"Federico","last_name":"Napoli","full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b"},{"first_name":"Anna","full_name":"Kapitonova, Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova"},{"last_name":"Tatman","full_name":"Tatman, Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin"},{"full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker","first_name":"Roman J."},{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"isi":1,"external_id":{"isi":["001618289100020"]},"_id":"20258","issue":"23","volume":437,"intvolume":"       437"},{"date_published":"2025-12-01T00:00:00Z","pmid":1,"article_processing_charge":"Yes (in subscription journal)","ddc":["540"],"project":[{"_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","grant_number":"I06223","name":"Structure and mechanism of the mitochondrial MIM insertase"},{"name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"publisher":"Elsevier","year":"2025","article_number":"169465","_id":"20538","issue":"23","external_id":{"pmid":["41016549"]},"author":[{"last_name":"Knödlstorfer","full_name":"Knödlstorfer, Sonja","first_name":"Sonja"},{"first_name":"Giorgia","last_name":"Toscano","full_name":"Toscano, Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4"},{"full_name":"Ptaszek, Aleksandra L.","last_name":"Ptaszek","first_name":"Aleksandra L."},{"first_name":"Georg","full_name":"Kontaxis, Georg","last_name":"Kontaxis"},{"orcid":"0000-0002-9043-136X","first_name":"Federico","full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","last_name":"Napoli"},{"first_name":"Jakob","full_name":"Schneider, Jakob","id":"64368429-eb97-11eb-a6c2-c980b1f44415","last_name":"Schneider"},{"full_name":"Maier, Katharina","last_name":"Maier","first_name":"Katharina"},{"last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna","first_name":"Anna"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"},{"full_name":"Konrat, Robert","last_name":"Konrat","first_name":"Robert"}],"intvolume":"       437","volume":437,"department":[{"_id":"PaSc"},{"_id":"GradSch"}],"publication_status":"published","day":"01","doi":"10.1016/j.jmb.2025.169465","month":"12","quality_controlled":"1","oa_version":"Published Version","language":[{"iso":"eng"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"file":[{"file_name":"2025_JourMolecularBiology_Knoedlstorfer.pdf","file_id":"20915","date_created":"2025-12-30T10:29:08Z","creator":"dernst","file_size":3076611,"date_updated":"2025-12-30T10:29:08Z","access_level":"open_access","success":1,"checksum":"feb92f9c79032c261165f4ca573f444a","relation":"main_file","content_type":"application/pdf"}],"citation":{"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).","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.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169465, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>.","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.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>.","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.","ieee":"S. Knödlstorfer <i>et al.</i>, “A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","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. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>","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. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>"},"status":"public","scopus_import":"1","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.","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0","OA_type":"hybrid","article_type":"original","OA_place":"publisher","oa":1,"has_accepted_license":"1","publication":"Journal of Molecular Biology","date_created":"2025-10-26T23:01:35Z","publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"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."}],"type":"journal_article","date_updated":"2025-12-30T10:29:20Z","PlanS_conform":"1","file_date_updated":"2025-12-30T10:29:08Z"}]