{"_id":"19956","contributor":[{"first_name":"Darja","last_name":"Rohden","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Napoli","first_name":"Federico"},{"contributor_type":"researcher","last_name":"Tatman","first_name":"Ben"},{"contributor_type":"researcher","last_name":"Schanda","first_name":"Paul"}],"date_updated":"2025-08-14T10:52:36Z","date_created":"2025-07-03T04:21:37Z","month":"07","title":"Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme","oa":1,"ddc":["572"],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publisher":"Institute of Science and Technology Austria","has_accepted_license":"1","oa_version":"None","file_date_updated":"2025-08-14T07:06:58Z","day":"03","article_processing_charge":"No","citation":{"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>.","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>.","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>","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."},"file":[{"file_name":"README","file_size":1160,"file_id":"19960","content_type":"application/octet-stream","success":1,"access_level":"open_access","relation":"main_file","date_updated":"2025-07-03T10:30:14Z","checksum":"a2ef61aa9fb5313c7d426913eb0482c0","creator":"pschanda","date_created":"2025-07-03T10:30:14Z"},{"file_name":"data_Arg_MASNMR_Rohden.zip","content_type":"application/zip","file_id":"19961","file_size":128597184,"success":1,"access_level":"open_access","relation":"main_file","date_updated":"2025-07-03T10:30:55Z","checksum":"8fb77b96d0fcc95c9903005652207a8c","date_created":"2025-07-03T10:30:55Z","creator":"pschanda"},{"success":1,"access_level":"open_access","file_name":"20240903_ubi_DN_Argd1C13_2D_spectra.tar.xz","file_size":4766564,"file_id":"20172","content_type":"application/x-xz","checksum":"a60cc16d20b089c4bef94040a99cfba5","creator":"pschanda","date_created":"2025-08-14T07:06:58Z","relation":"main_file","date_updated":"2025-08-14T07:06:58Z"}],"project":[{"name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812"}],"author":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606"}],"corr_author":"1","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"}],"type":"research_data","doi":"10.15479/AT-ISTA-19956","department":[{"_id":"PaSc"}],"date_published":"2025-07-03T00:00:00Z","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","status":"public","tmp":{"short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"year":"2025"}