[{"type":"journal_article","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.","publication_identifier":{"issn":["0022-2836"],"eissn":["1089-8638"]},"status":"public","volume":437,"OA_place":"publisher","issue":"23","doi":"10.1016/j.jmb.2025.169465","has_accepted_license":"1","PlanS_conform":"1","year":"2025","oa":1,"file":[{"file_id":"20915","access_level":"open_access","creator":"dernst","success":1,"date_created":"2025-12-30T10:29:08Z","relation":"main_file","date_updated":"2025-12-30T10:29:08Z","file_name":"2025_JourMolecularBiology_Knoedlstorfer.pdf","checksum":"feb92f9c79032c261165f4ca573f444a","content_type":"application/pdf","file_size":3076611}],"language":[{"iso":"eng"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"month":"12","license":"https://creativecommons.org/licenses/by/4.0/","day":"01","_id":"20538","article_processing_charge":"Yes (in subscription journal)","oa_version":"Published Version","scopus_import":"1","article_type":"original","intvolume":"       437","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publisher":"Elsevier","quality_controlled":"1","citation":{"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>","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>","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.","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>.","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."},"ddc":["540"],"OA_type":"hybrid","date_published":"2025-12-01T00:00:00Z","article_number":"169465","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","pmid":1,"publication":"Journal of Molecular Biology","file_date_updated":"2025-12-30T10:29:08Z","date_updated":"2025-12-30T10:29:20Z","abstract":[{"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.","lang":"eng"}],"project":[{"_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","name":"Structure and mechanism of the mitochondrial MIM insertase","grant_number":"I06223"},{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"external_id":{"pmid":["41016549"]},"date_created":"2025-10-26T23:01:35Z","title":"A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0","author":[{"first_name":"Sonja","last_name":"Knödlstorfer","full_name":"Knödlstorfer, Sonja"},{"first_name":"Giorgia","last_name":"Toscano","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","full_name":"Toscano, Giorgia"},{"last_name":"Ptaszek","first_name":"Aleksandra L.","full_name":"Ptaszek, Aleksandra L."},{"full_name":"Kontaxis, Georg","last_name":"Kontaxis","first_name":"Georg"},{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","full_name":"Napoli, Federico","last_name":"Napoli","first_name":"Federico","orcid":"0000-0002-9043-136X"},{"full_name":"Schneider, Jakob","id":"64368429-eb97-11eb-a6c2-c980b1f44415","last_name":"Schneider","first_name":"Jakob"},{"full_name":"Maier, Katharina","last_name":"Maier","first_name":"Katharina"},{"full_name":"Kapitonova, Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova","first_name":"Anna"},{"first_name":"Roman J.","last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J."},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Robert","last_name":"Konrat","full_name":"Konrat, Robert"}]},{"intvolume":"        31","department":[{"_id":"PaSc"}],"scopus_import":"1","article_type":"original","_id":"19555","article_processing_charge":"Yes (in subscription journal)","oa_version":"Published Version","day":"25","ddc":["540"],"quality_controlled":"1","citation":{"short":"D. Rohden, G. Toscano, P. Schanda, R.J. Lichtenecker, Chemistry - A European Journal 31 (2025).","mla":"Rohden, Darja, et al. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” <i>Chemistry - A European Journal</i>, vol. 31, no. 24, e202500408, Wiley, 2025, doi:<a href=\"https://doi.org/10.1002/chem.202500408\">10.1002/chem.202500408</a>.","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,” <i>Chemistry - A European Journal</i>, 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.","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.” <i>Chemistry - A European Journal</i>. Wiley, 2025. <a href=\"https://doi.org/10.1002/chem.202500408\">https://doi.org/10.1002/chem.202500408</a>.","apa":"Rohden, D., Toscano, G., Schanda, P., &#38; Lichtenecker, R. J. (2025). Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. <i>Chemistry - A European Journal</i>. Wiley. <a href=\"https://doi.org/10.1002/chem.202500408\">https://doi.org/10.1002/chem.202500408</a>","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. <i>Chemistry - A European Journal</i>. 2025;31(24). doi:<a href=\"https://doi.org/10.1002/chem.202500408\">10.1002/chem.202500408</a>"},"publisher":"Wiley","acknowledged_ssus":[{"_id":"NMR"}],"publication":"Chemistry - A European Journal","file_date_updated":"2025-08-05T12:59:24Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","pmid":1,"publication_status":"published","article_number":"e202500408","corr_author":"1","OA_type":"hybrid","date_published":"2025-04-25T00:00:00Z","date_created":"2025-04-13T22:01:19Z","external_id":{"pmid":["40080421"],"isi":["001479486400019"]},"title":"Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy","author":[{"first_name":"Darja","last_name":"Rohden","full_name":"Rohden, Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3"},{"full_name":"Toscano, Giorgia","last_name":"Toscano","first_name":"Giorgia"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"first_name":"Roman J.","last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J."}],"project":[{"name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"abstract":[{"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.","lang":"eng"}],"date_updated":"2025-09-30T11:35:05Z","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.","type":"journal_article","volume":31,"OA_place":"publisher","status":"public","publication_identifier":{"issn":["0947-6539"],"eissn":["1521-3765"]},"language":[{"iso":"eng"}],"file":[{"file_name":"2025_ChemistryEur_Rohden.pdf","date_updated":"2025-08-05T12:59:24Z","checksum":"e3788628644b5aac666cf079b05f8fa7","file_size":2840681,"content_type":"application/pdf","relation":"main_file","date_created":"2025-08-05T12:59:24Z","creator":"dernst","success":1,"access_level":"open_access","file_id":"20136"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2025","oa":1,"doi":"10.1002/chem.202500408","issue":"24","has_accepted_license":"1","PlanS_conform":"1","month":"04","isi":1},{"year":"2025","oa":1,"file":[{"date_created":"2026-02-19T08:56:10Z","relation":"main_file","checksum":"f33230a6d59b7978d4cd72795e4e9059","content_type":"application/pdf","file_size":1924177,"file_name":"2025_ICML_Maddipatla.pdf","date_updated":"2026-02-19T08:56:10Z","file_id":"21338","access_level":"open_access","success":1,"creator":"dernst"}],"language":[{"iso":"eng"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"has_accepted_license":"1","conference":{"start_date":"2025-07-13","name":"ICML: International Conference on Machine Learning","end_date":"2025-07-19","location":"Vancouver, Canada"},"page":"42366 - 42393","month":"07","arxiv":1,"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. ","type":"conference","volume":267,"OA_place":"publisher","publication_identifier":{"eissn":["2640-3498"]},"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","publication":"Proceedings of the 42nd International Conference on Machine Learning","file_date_updated":"2026-02-19T08:56:10Z","OA_type":"gold","date_published":"2025-07-30T00:00:00Z","corr_author":"1","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"},{"name":"Structure and mechanism of the mitochondrial MIM insertase","grant_number":"I06223","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0"}],"date_created":"2026-02-18T12:11:17Z","external_id":{"arxiv":["2502.09372"]},"title":"Inverse problems with experiment-guided AlphaFold","author":[{"id":"e957f5e5-91c9-11f0-a95f-e090f66ecb4d","full_name":"Maddipatla, Sai A","last_name":"Maddipatla","first_name":"Sai A"},{"id":"ef280fe0-91c9-11f0-a95f-8dea3f5bc513","full_name":"Sellam, Nadav E","first_name":"Nadav E","last_name":"Sellam"},{"first_name":"Meital I","last_name":"Bojan","id":"11d88cf5-91ca-11f0-a95f-edf9f08f47b7","full_name":"Bojan, Meital I"},{"last_name":"Vedula","first_name":"Sanketh","id":"94f2fe44-70fa-11f0-b76b-92922c09452b","full_name":"Vedula, Sanketh"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Ailie","last_name":"Marx","full_name":"Marx, Ailie"},{"full_name":"Bronstein, Alexander","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6","last_name":"Bronstein","first_name":"Alexander","orcid":"0000-0001-9699-8730"}],"date_updated":"2026-02-19T08:56:43Z","abstract":[{"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.","lang":"eng"}],"intvolume":"       267","department":[{"_id":"PaSc"},{"_id":"AlBr"},{"_id":"GradSch"}],"alternative_title":["PMLR"],"day":"30","_id":"21327","oa_version":"Published Version","article_processing_charge":"No","quality_controlled":"1","citation":{"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.","ieee":"S. A. Maddipatla <i>et al.</i>, “Inverse problems with experiment-guided AlphaFold,” in <i>Proceedings of the 42nd International Conference on Machine Learning</i>, Vancouver, Canada, 2025, vol. 267, pp. 42366–42393.","mla":"Maddipatla, Sai A., et al. “Inverse Problems with Experiment-Guided AlphaFold.” <i>Proceedings of the 42nd International Conference on Machine Learning</i>, 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.","apa":"Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Vedula, S., Schanda, P., Marx, A., &#38; Bronstein, A. M. (2025). Inverse problems with experiment-guided AlphaFold. In <i>Proceedings of the 42nd International Conference on Machine Learning</i> (Vol. 267, pp. 42366–42393). Vancouver, Canada: ML Research Press.","ama":"Maddipatla SA, Sellam NE, Bojan MI, et al. Inverse problems with experiment-guided AlphaFold. In: <i>Proceedings of the 42nd International Conference on Machine Learning</i>. Vol 267. ML Research Press; 2025:42366-42393.","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 <i>Proceedings of the 42nd International Conference on Machine Learning</i>, 267:42366–93. ML Research Press, 2025."},"ddc":["000","540"],"acknowledged_ssus":[{"_id":"ScienComp"}],"publisher":"ML Research Press"},{"status":"public","publication_identifier":{"issn":["0022-2836"],"eissn":["1089-8638"]},"volume":437,"OA_place":"publisher","type":"journal_article","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.","isi":1,"month":"12","issue":"23","doi":"10.1016/j.jmb.2025.169379","has_accepted_license":"1","PlanS_conform":"1","related_material":{"record":[{"id":"19956","status":"public","relation":"research_data"}]},"language":[{"iso":"eng"}],"file":[{"file_id":"20876","creator":"dernst","success":1,"access_level":"open_access","relation":"main_file","date_created":"2025-12-29T14:51:40Z","file_name":"2025_JourMolecularBiology_Rohden.pdf","date_updated":"2025-12-29T14:51:40Z","content_type":"application/pdf","checksum":"90d50594d8ea9860ac5da41297992847","file_size":2270555}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2025","oa":1,"publisher":"Elsevier","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"ddc":["540"],"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).","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>.","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.","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>","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>","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>."},"quality_controlled":"1","_id":"20258","oa_version":"Published Version","article_processing_charge":"Yes (via OA deal)","day":"01","intvolume":"       437","department":[{"_id":"PaSc"}],"scopus_import":"1","article_type":"original","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"}],"date_updated":"2026-06-10T08:20:37Z","external_id":{"isi":["001618289100020"]},"date_created":"2025-08-31T22:01:33Z","title":"Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme","author":[{"last_name":"Rohden","first_name":"Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","full_name":"Rohden, Darja"},{"full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","last_name":"Napoli","first_name":"Federico","orcid":"0000-0002-9043-136X"},{"full_name":"Kapitonova, Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova","first_name":"Anna"},{"id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin","first_name":"Benjamin","last_name":"Tatman"},{"full_name":"Lichtenecker, Roman J.","first_name":"Roman J.","last_name":"Lichtenecker"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"project":[{"grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"article_number":"169379","corr_author":"1","OA_type":"hybrid","date_published":"2025-12-01T00:00:00Z","file_date_updated":"2025-12-29T14:51:40Z","publication":"Journal of Molecular Biology","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published"},{"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publisher":"Institute of Science and Technology Austria","citation":{"apa":"Schanda, P. (2025). Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">https://doi.org/10.15479/AT-ISTA-19956</a>","ama":"Schanda P. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>","chicago":"Schanda, Paul. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">https://doi.org/10.15479/AT-ISTA-19956</a>.","ista":"Schanda P. 2025. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>.","ieee":"P. Schanda, “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025.","short":"P. Schanda, (2025).","mla":"Schanda, Paul. <i>Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme</i>. Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>."},"ddc":["572"],"day":"03","_id":"19956","article_processing_charge":"No","oa_version":"Published Version","department":[{"_id":"PaSc"}],"date_updated":"2026-06-10T08:20:38Z","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"}],"project":[{"name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"date_created":"2025-07-03T04:21:37Z","title":"Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme","author":[{"orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"date_published":"2025-07-03T00:00:00Z","corr_author":"1","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","file_date_updated":"2025-08-14T07:06:58Z","status":"public","type":"research_data","contributor":[{"contributor_type":"researcher","last_name":"Rohden","first_name":"Darja"},{"first_name":"Federico","last_name":"Napoli","contributor_type":"researcher"},{"last_name":"Tatman","first_name":"Ben","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Schanda","first_name":"Paul"}],"month":"07","license":"https://creativecommons.org/licenses/by-nc/4.0/","doi":"10.15479/AT-ISTA-19956","has_accepted_license":"1","related_material":{"record":[{"relation":"used_in_publication","id":"20258","status":"public"}]},"year":"2025","oa":1,"file":[{"date_created":"2025-07-03T10:30:14Z","relation":"main_file","checksum":"a2ef61aa9fb5313c7d426913eb0482c0","file_size":1160,"content_type":"application/octet-stream","file_name":"README","date_updated":"2025-07-03T10:30:14Z","file_id":"19960","access_level":"open_access","success":1,"creator":"pschanda"},{"access_level":"open_access","creator":"pschanda","success":1,"file_id":"19961","file_name":"data_Arg_MASNMR_Rohden.zip","date_updated":"2025-07-03T10:30:55Z","content_type":"application/zip","file_size":128597184,"checksum":"8fb77b96d0fcc95c9903005652207a8c","date_created":"2025-07-03T10:30:55Z","relation":"main_file"},{"file_name":"20240903_ubi_DN_Argd1C13_2D_spectra.tar.xz","date_updated":"2025-08-14T07:06:58Z","content_type":"application/x-xz","checksum":"a60cc16d20b089c4bef94040a99cfba5","file_size":4766564,"date_created":"2025-08-14T07:06:58Z","relation":"main_file","access_level":"open_access","creator":"pschanda","success":1,"file_id":"20172"}],"tmp":{"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)","image":"/images/cc_by_nc.png"}},{"doi":"10.1146/annurev-biophys-070323-022428","page":"247-273","has_accepted_license":"1","year":"2024","oa":1,"language":[{"iso":"eng"}],"file":[{"file_id":"18911","access_level":"open_access","success":1,"creator":"dernst","date_created":"2025-01-27T13:44:59Z","relation":"main_file","checksum":"c90861542ae3f9147939030d5bafed3c","file_size":3025589,"content_type":"application/pdf","file_name":"2024_AnnualReviews_Schanda.pdf","date_updated":"2025-01-27T13:44:59Z"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"isi":1,"month":"07","type":"journal_article","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.","publication_identifier":{"issn":["1936-122X"],"eissn":["1936-1238"]},"status":"public","volume":53,"OA_place":"publisher","OA_type":"hybrid","date_published":"2024-07-01T00:00:00Z","corr_author":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication_status":"published","pmid":1,"publication":"Annual Review of Biophysics","file_date_updated":"2025-01-27T13:44:59Z","date_updated":"2025-09-09T12:06:24Z","abstract":[{"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.","lang":"eng"}],"project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"date_created":"2025-01-27T13:40:34Z","external_id":{"pmid":["38346243"],"isi":["001278237500012"]},"author":[{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"last_name":"Haran","first_name":"Gilad","full_name":"Haran, Gilad"}],"title":"NMR and single-molecule FRET insights into fast protein motions and their relation to function","day":"01","_id":"18910","article_processing_charge":"No","oa_version":"Published Version","article_type":"original","scopus_import":"1","intvolume":"        53","department":[{"_id":"PaSc"}],"publisher":"Annual Reviews","citation":{"chicago":"Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” <i>Annual Review of Biophysics</i>. Annual Reviews, 2024. <a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">https://doi.org/10.1146/annurev-biophys-070323-022428</a>.","ama":"Schanda P, Haran G. NMR and single-molecule FRET insights into fast protein motions and their relation to function. <i>Annual Review of Biophysics</i>. 2024;53:247-273. doi:<a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">10.1146/annurev-biophys-070323-022428</a>","apa":"Schanda, P., &#38; Haran, G. (2024). NMR and single-molecule FRET insights into fast protein motions and their relation to function. <i>Annual Review of Biophysics</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">https://doi.org/10.1146/annurev-biophys-070323-022428</a>","ieee":"P. Schanda and G. Haran, “NMR and single-molecule FRET insights into fast protein motions and their relation to function,” <i>Annual Review of Biophysics</i>, vol. 53. Annual Reviews, pp. 247–273, 2024.","short":"P. Schanda, G. Haran, Annual Review of Biophysics 53 (2024) 247–273.","mla":"Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” <i>Annual Review of Biophysics</i>, vol. 53, Annual Reviews, 2024, pp. 247–73, doi:<a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">10.1146/annurev-biophys-070323-022428</a>.","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."},"quality_controlled":"1","ddc":["570"]},{"quality_controlled":"1","citation":{"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.","ieee":"F. Napoli <i>et al.</i>, “Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck,” <i>Magnetic Resonance</i>, vol. 5, no. 1. Copernicus Publications, pp. 33–49, 2024.","short":"F. Napoli, J.-Y. Guan, C.-A. Arnaud, P. Macek, H. Fraga, C. Breyton, P. Schanda, Magnetic Resonance 5 (2024) 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.” <i>Magnetic Resonance</i>, vol. 5, no. 1, Copernicus Publications, 2024, pp. 33–49, doi:<a href=\"https://doi.org/10.5194/mr-5-33-2024\">10.5194/mr-5-33-2024</a>.","apa":"Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C., &#38; Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-5-33-2024\">https://doi.org/10.5194/mr-5-33-2024</a>","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. <i>Magnetic Resonance</i>. 2024;5(1):33-49. doi:<a href=\"https://doi.org/10.5194/mr-5-33-2024\">10.5194/mr-5-33-2024</a>","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.” <i>Magnetic Resonance</i>. Copernicus Publications, 2024. <a href=\"https://doi.org/10.5194/mr-5-33-2024\">https://doi.org/10.5194/mr-5-33-2024</a>."},"ddc":["530"],"acknowledged_ssus":[{"_id":"NMR"}],"publisher":"Copernicus Publications","article_type":"original","scopus_import":"1","department":[{"_id":"PaSc"}],"intvolume":"         5","day":"19","oa_version":"Published Version","article_processing_charge":"Yes","_id":"15401","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"},{"name":"FWF Open Access Fund","call_identifier":"FWF","_id":"3AC91DDA-15DF-11EA-824D-93A3E7B544D1"}],"title":"Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck","author":[{"full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","last_name":"Napoli","first_name":"Federico","orcid":"0000-0002-9043-136X"},{"full_name":"Guan, Jia-Ying","first_name":"Jia-Ying","last_name":"Guan"},{"last_name":"Arnaud","first_name":"Charles-Adrien","full_name":"Arnaud, Charles-Adrien"},{"last_name":"Macek","first_name":"Pavel","full_name":"Macek, Pavel"},{"full_name":"Fraga, Hugo","last_name":"Fraga","first_name":"Hugo"},{"first_name":"Cécile","last_name":"Breyton","full_name":"Breyton, Cécile"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"date_created":"2024-05-16T15:02:43Z","external_id":{"pmid":["40384771"]},"date_updated":"2025-07-17T08:12:23Z","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."}],"publication_status":"published","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Magnetic Resonance","file_date_updated":"2024-05-22T07:01:15Z","date_published":"2024-04-19T00:00:00Z","OA_type":"gold","corr_author":"1","OA_place":"publisher","volume":5,"publication_identifier":{"issn":["2699-0016"]},"status":"public","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.","APC_amount":"1530 EUR","type":"journal_article","month":"04","oa":1,"year":"2024","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"language":[{"iso":"eng"}],"file":[{"date_updated":"2024-05-22T07:01:15Z","file_name":"2024_MagneticResonance_Napoli.pdf","content_type":"application/pdf","file_size":6657865,"checksum":"80ea50114e428461ca9530d3bd5d89e4","relation":"main_file","date_created":"2024-05-22T07:01:15Z","creator":"dernst","success":1,"access_level":"open_access","file_id":"15413"}],"page":"33-49","has_accepted_license":"1","doi":"10.5194/mr-5-33-2024","issue":"1"},{"volume":82,"publication_identifier":{"eissn":["1879-033X"],"issn":["0959-440X"]},"status":"public","acknowledgement":"We thank Petra Rovó for critical reading of this manuscript. We acknowledge the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding by the Institute of Science and Technology Austria.","type":"journal_article","month":"10","isi":1,"oa":1,"year":"2023","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"file":[{"file_size":1231998,"checksum":"c850f7ac8a4234319755b672c1df69ae","content_type":"application/pdf","file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","date_updated":"2024-01-30T12:36:39Z","relation":"main_file","date_created":"2024-01-30T12:36:39Z","success":1,"creator":"dernst","access_level":"open_access","file_id":"14907"}],"language":[{"iso":"eng"}],"issue":"10","doi":"10.1016/j.sbi.2023.102660","citation":{"ista":"Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10), 102660.","short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).","mla":"Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10, 102660, Elsevier, 2023, doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>.","ieee":"F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle spinning relaxation dispersion NMR,” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10. Elsevier, 2023.","ama":"Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10). doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>","apa":"Napoli, F., Becker, L. M., &#38; Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>","chicago":"Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>."},"quality_controlled":"1","ddc":["570"],"publisher":"Elsevier","scopus_import":"1","article_type":"original","department":[{"_id":"PaSc"}],"intvolume":"        82","day":"01","oa_version":"Published Version","article_processing_charge":"Yes (via OA deal)","_id":"14036","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","author":[{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","full_name":"Napoli, Federico","orcid":"0000-0002-9043-136X","first_name":"Federico","last_name":"Napoli"},{"first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"date_created":"2023-08-13T22:01:11Z","external_id":{"pmid":["37536064"],"isi":["001053616200001"]},"date_updated":"2025-04-14T09:10:17Z","abstract":[{"text":"Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has a wider arsenal of observables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large enzymes, membrane proteins, and protein assemblies.","lang":"eng"}],"publication_status":"published","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Current Opinion in Structural Biology","file_date_updated":"2024-01-30T12:36:39Z","date_published":"2023-10-01T00:00:00Z","corr_author":"1","article_number":"102660"}]