[{"ddc":["540"],"language":[{"iso":"eng"}],"doi":"10.1016/j.pnmrs.2026.101615","acknowledgement":"We thank the Austrian Science Fund (FWF, project number 10.55776/I5812) for support. We are grateful to Petra Rovó (ISTA) for many insightful discussions.","date_created":"2026-09-22T05:44:22Z","keyword":["Solid-state NMR","Protein dynamics","Magic-angle spinning"],"quality_controlled":"1","article_number":"101615","publication":"Progress in Nuclear Magnetic Resonance Spectroscopy","citation":{"short":"B. Tatman, P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 156–157 (2026).","ista":"Tatman B, Schanda P. 2026. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. Progress in Nuclear Magnetic Resonance Spectroscopy. 156–157, 101615.","mla":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157, 101615, Elsevier, 2026, doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>.","ieee":"B. Tatman and P. Schanda, “Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches,” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157. Elsevier, 2026.","ama":"Tatman B, Schanda P. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. 2026;156-157. doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>","chicago":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier, 2026. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>.","apa":"Tatman, B., &#38; Schanda, P. (2026). Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>"},"volume":"156-157","_id":"22974","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"url":"https://doi.org/10.1016/j.pnmrs.2026.101615","open_access":"1"}],"OA_type":"hybrid","oa":1,"title":"Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches","scopus_import":"1","date_updated":"2026-10-06T13:00:47Z","publication_status":"epub_ahead","dataavailabilitystatement":"No data was used for the research described in the article.","status":"public","date_published":"2026-09-01T00:00:00Z","type":"journal_article","month":"09","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"abstract":[{"text":"Far from being static structures, it is now well accepted that proteins are highly dynamic entities even in the solid state. Here, we review recent progress in application of magic-angle spinning (MAS) NMR for studying the site-specific dynamics of proteins, as assessed using spin-relaxation and measurement of anisotropic spin interactions. We focus on the types of experimental data that are available, and how best to access the information which is provided by these experimental measurements; in particular, we provide a retrospective on the field in light of recent advances in analytical methodologies, which have led to a slow paradigm shift in how we interpret relaxation rate constant measurements made in the solid state.","lang":"eng"}],"article_processing_charge":"Yes (via OA deal)","year":"2026","publisher":"Elsevier","article_type":"original","researchdata_availability":"no","department":[{"_id":"PaSc"}],"author":[{"full_name":"Tatman, Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda"}],"OA_place":"publisher","corr_author":"1","fulldoi":"https://doi.org/10.1016/j.pnmrs.2026.101615","has_accepted_license":"1","day":"01","das_tickbox":"1","publication_identifier":{"issn":["0079-6565"],"eissn":["1873-3301"]},"supplementarymaterial":"yes","tmp":{"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)","image":"/images/cc_by.png"},"oa_version":"Published Version"},{"contributor":[{"first_name":"Alicia","contributor_type":"data_collector","last_name":"Vallet"},{"contributor_type":"data_collector","last_name":"Ayala","first_name":"Isabel "},{"last_name":"Perrone","contributor_type":"data_collector","first_name":"Barbara"},{"last_name":"Hassan","contributor_type":"data_collector","first_name":"Alia"},{"first_name":"Catherine","contributor_type":"data_collector","last_name":"Bougault"}],"date_created":"2024-05-22T12:04:54Z","keyword":["nuclear magnetic resonance","NMR","cellwall","structural biology","spectroscopy"],"month":"05","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","year":"2024","publisher":"Institute of Science and Technology Austria","ddc":["570"],"date_published":"2024-05-22T00:00:00Z","status":"public","file_date_updated":"2024-05-22T12:17:10Z","doi":"10.15479/AT:ISTA:17042","type":"research_data","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","day":"22","title":"Raw data to \"MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments\"","oa":1,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)"},"oa_version":"Published Version","date_updated":"2025-09-09T12:01:41Z","related_material":{"record":[{"status":"public","id":"17291","relation":"used_in_publication"}]},"file":[{"access_level":"open_access","date_created":"2024-05-22T12:05:13Z","date_updated":"2024-05-22T12:05:13Z","relation":"main_file","content_type":"text/plain","file_name":"Read_me.txt","file_id":"17043","file_size":2132,"success":1,"creator":"pschanda","checksum":"eb55f0988342d927702353b75e07edfa"},{"success":1,"creator":"pschanda","checksum":"3393592acaf5ee1e032052c236780914","access_level":"open_access","date_created":"2024-05-22T12:17:10Z","date_updated":"2024-05-22T12:17:10Z","content_type":"application/zip","file_name":"raw_data_CryoMAS_cyronebacteria.zip","relation":"main_file","file_size":755704888,"file_id":"17044"}],"citation":{"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. <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">https://doi.org/10.15479/AT:ISTA:17042</a>","ama":"Schanda P. Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” 2024. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>","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. <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">https://doi.org/10.15479/AT:ISTA:17042</a>.","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.","mla":"Schanda, Paul. <i>Raw Data to “MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.”</i> Institute of Science and Technology Austria, 2024, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>.","short":"P. Schanda, (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, <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>."},"department":[{"_id":"PaSc"}],"author":[{"last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul"}],"_id":"17042","corr_author":"1","fulldoi":"https://doi.org/10.15479/AT:ISTA:17042"},{"issue":"2","pmid":1,"external_id":{"pmid":["26786064"]},"quality_controlled":"1","date_created":"2018-12-11T11:46:02Z","keyword":["NMR","CsPbBr3","absorption coefficient","surface chemistry"],"doi":"10.1021/acsnano.5b06295","language":[{"iso":"eng"}],"intvolume":"        10","scopus_import":"1","date_updated":"2026-05-13T14:05:15Z","title":"Highly dynamic ligand binding and light absorption coefficient of cesium lead bromide perovskite nanocrystals","OA_type":"closed access","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","page":"2071 - 2081","_id":"363","volume":10,"citation":{"apa":"De Roo, J., Ibáñez, M., Geiregat, P., Nedelcu, G., Walravens, W., Maes, J., … Hens, Z. (2016). Highly dynamic ligand binding and light absorption coefficient of cesium lead bromide perovskite nanocrystals. <i>Nano</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acsnano.5b06295\">https://doi.org/10.1021/acsnano.5b06295</a>","chicago":"De Roo, Jonathan, Maria Ibáñez, Pieter Geiregat, Georgian Nedelcu, Willem Walravens, Jorick Maes, Jose Martins, Isabel Van Driessche, Maksym Kovalenko, and Zeger Hens. “Highly Dynamic Ligand Binding and Light Absorption Coefficient of Cesium Lead Bromide Perovskite Nanocrystals.” <i>Nano</i>. American Chemical Society, 2016. <a href=\"https://doi.org/10.1021/acsnano.5b06295\">https://doi.org/10.1021/acsnano.5b06295</a>.","ama":"De Roo J, Ibáñez M, Geiregat P, et al. Highly dynamic ligand binding and light absorption coefficient of cesium lead bromide perovskite nanocrystals. <i>Nano</i>. 2016;10(2):2071-2081. doi:<a href=\"https://doi.org/10.1021/acsnano.5b06295\">10.1021/acsnano.5b06295</a>","mla":"De Roo, Jonathan, et al. “Highly Dynamic Ligand Binding and Light Absorption Coefficient of Cesium Lead Bromide Perovskite Nanocrystals.” <i>Nano</i>, vol. 10, no. 2, American Chemical Society, 2016, pp. 2071–81, doi:<a href=\"https://doi.org/10.1021/acsnano.5b06295\">10.1021/acsnano.5b06295</a>.","ieee":"J. De Roo <i>et al.</i>, “Highly dynamic ligand binding and light absorption coefficient of cesium lead bromide perovskite nanocrystals,” <i>Nano</i>, vol. 10, no. 2. American Chemical Society, pp. 2071–2081, 2016.","ista":"De Roo J, Ibáñez M, Geiregat P, Nedelcu G, Walravens W, Maes J, Martins J, Van Driessche I, Kovalenko M, Hens Z. 2016. Highly dynamic ligand binding and light absorption coefficient of cesium lead bromide perovskite nanocrystals. Nano. 10(2), 2071–2081.","short":"J. De Roo, M. Ibáñez, P. Geiregat, G. Nedelcu, W. Walravens, J. Maes, J. Martins, I. Van Driessche, M. Kovalenko, Z. Hens, Nano 10 (2016) 2071–2081."},"publication":"Nano","article_processing_charge":"No","year":"2016","publisher":"American Chemical Society","abstract":[{"text":"Lead halide perovskite materials have attracted significant attention in the context of photovoltaics and other optoelectronic applications, and recently, research efforts have been directed to nanostructured lead halide perovskites. Collodial nanocrystals (NCs) of cesium lead halides (CsPbX3, X = Cl, Br, I) exhibit bright photoluminescence, with emission tunable over the entire visible spectral region. However, previous studies on CsPbX3 NCs did not address key aspects of their chemistry and photophysics such as surface chemistry and quantitative light absorption. Here, we elaborate on the synthesis of CsPbBr3 NCs and their surface chemistry. In addition, the intrinsic absorption coefficient was determined experimentally by combining elemental analysis with accurate optical absorption measurements. 1H solution nuclear magnetic resonance spectroscopy was used to characterize sample purity, elucidate the surface chemistry, and evaluate the influence of purification methods on the surface composition. We find that ligand binding to the NC surface is highly dynamic, and therefore, ligands are easily lost during the isolation and purification procedures. However, when a small amount of both oleic acid and oleylamine is added, the NCs can be purified, maintaining optical, colloidal, and material integrity. In addition, we find that a high amine content in the ligand shell increases the quantum yield due to the improved binding of the carboxylic acid.","lang":"eng"}],"month":"02","type":"journal_article","date_published":"2016-02-23T00:00:00Z","status":"public","publication_status":"published","oa_version":"None","publication_identifier":{"eissn":["1936-086X"],"issn":["1936-0851"]},"publist_id":"7464","extern":"1","day":"23","fulldoi":"https://doi.org/10.1021/acsnano.5b06295","author":[{"last_name":"De Roo","full_name":"De Roo, Jonathan","first_name":"Jonathan"},{"id":"43C61214-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-5013-2843","first_name":"Maria","full_name":"Ibáñez, Maria","last_name":"Ibáñez"},{"first_name":"Pieter","last_name":"Geiregat","full_name":"Geiregat, Pieter"},{"full_name":"Nedelcu, Georgian","last_name":"Nedelcu","first_name":"Georgian"},{"last_name":"Walravens","full_name":"Walravens, Willem","first_name":"Willem"},{"first_name":"Jorick","last_name":"Maes","full_name":"Maes, Jorick"},{"last_name":"Martins","full_name":"Martins, Jose","first_name":"Jose"},{"last_name":"Van Driessche","full_name":"Van Driessche, Isabel","first_name":"Isabel"},{"last_name":"Kovalenko","full_name":"Kovalenko, Maksym","first_name":"Maksym"},{"last_name":"Hens","full_name":"Hens, Zeger","first_name":"Zeger"}],"article_type":"original"}]