{"citation":{"short":"D. Rohden, F. Napoli, R.J. Lichtenecker, P. Schanda, ACS Chemical Biology (2026).","ista":"Rohden D, Napoli F, Lichtenecker RJ, Schanda P. 2026. Chemoenzymatic proline isotope labeling for solution and magic-angle spinning protein nuclear magnetic resonance. ACS Chemical Biology.","mla":"Rohden, Darja, et al. “Chemoenzymatic Proline Isotope Labeling for Solution and Magic-Angle Spinning Protein Nuclear Magnetic Resonance.” <i>ACS Chemical Biology</i>, American Chemical Society, 2026, doi:<a href=\"https://doi.org/10.1021/acschembio.6c00587\">10.1021/acschembio.6c00587</a>.","chicago":"Rohden, Darja, Federico Napoli, Roman J. Lichtenecker, and Paul Schanda. “Chemoenzymatic Proline Isotope Labeling for Solution and Magic-Angle Spinning Protein Nuclear Magnetic Resonance.” <i>ACS Chemical Biology</i>. American Chemical Society, 2026. <a href=\"https://doi.org/10.1021/acschembio.6c00587\">https://doi.org/10.1021/acschembio.6c00587</a>.","ieee":"D. Rohden, F. Napoli, R. J. Lichtenecker, and P. Schanda, “Chemoenzymatic proline isotope labeling for solution and magic-angle spinning protein nuclear magnetic resonance,” <i>ACS Chemical Biology</i>. American Chemical Society, 2026.","ama":"Rohden D, Napoli F, Lichtenecker RJ, Schanda P. Chemoenzymatic proline isotope labeling for solution and magic-angle spinning protein nuclear magnetic resonance. <i>ACS Chemical Biology</i>. 2026. doi:<a href=\"https://doi.org/10.1021/acschembio.6c00587\">10.1021/acschembio.6c00587</a>","apa":"Rohden, D., Napoli, F., Lichtenecker, R. J., &#38; Schanda, P. (2026). Chemoenzymatic proline isotope labeling for solution and magic-angle spinning protein nuclear magnetic resonance. <i>ACS Chemical Biology</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acschembio.6c00587\">https://doi.org/10.1021/acschembio.6c00587</a>"},"ddc":["540"],"author":[{"last_name":"Rohden","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","first_name":"Darja","full_name":"Rohden, Darja"},{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","orcid":"0000-0002-9043-136X","last_name":"Napoli","full_name":"Napoli, Federico","first_name":"Federico"},{"full_name":"Lichtenecker, Roman J.","first_name":"Roman J.","last_name":"Lichtenecker"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul"}],"doi":"10.1021/acschembio.6c00587","publisher":"American Chemical Society","has_accepted_license":"1","abstract":[{"text":"The prevalence of proline residues in intrinsically disordered proteins, functional hinges of enzymes, and protein interaction sites highlights the importance of studying their local dynamics and interactions at atomic resolution. While nuclear magnetic resonance (NMR) spectroscopy is, in principle, ideally suited for such investigations, the absence of an amide proton precludes the use of conventional 1H–15N amide-detected experiments. 1H–13C-based approaches, though possible, remain challenging in large proteins. In this work, we present a selective labeling strategy that introduces an isolated 1H2δ–13Cδ–15N spin system in proline residues in otherwise deuterated proteins. Our method leverages the enzymatic conversion of ornithine, synthesized from cost-effective isotopic precursors. We demonstrate the utility of this approach by applying it to a 134 kDa enzyme using magic-angle spinning NMR, highlighting its potential to efficiently probe functionally relevant sites in proteins.","lang":"eng"}],"article_processing_charge":"Yes (via OA deal)","main_file_link":[{"url":"https://doi.org/10.1021/acschembio.6c00587","open_access":"1"}],"department":[{"_id":"PaSc"},{"_id":"GradSch"}],"publication_status":"epub_ahead","date_updated":"2026-10-19T11:20:33Z","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"month":"10","quality_controlled":"1","external_id":{"pmid":["42863127"]},"OA_type":"hybrid","date_created":"2026-10-19T11:12:28Z","das_tickbox":"1","OA_place":"publisher","status":"public","acknowledgement":"We thank Undina Guillerm, Rajkumar Singh and Anna Kapitonova for help with protein production. We are grateful to Dominique Madern for discussions and for providing the plasmid of IiMDH. We acknowledge the Scientific Service Units (SSU) of the Institute of Science and Technology Austria (ISTA) through resources provided by the NMR Facility and the Lab Support Facility, as well as the NMR centre and MS centre of the University of Vienna. This work was supported by the Austrian Science Fund (FWF; project number I5812-B) through a French-Austrian binational research project, as well as by the L’Oréal-UNESCO For Women in Science Fellowship, awarded in cooperation with the Austrian Academy of Sciences (ÖAW) and the Austrian Commission for UNESCO.","pmid":1,"dataavailabilitystatement":"Supporting Information is available free of charge at https://pubs.acs.org/10.1021/acschembio.6c00587.\r\n\r\nDetailed description of experimental methods; spectra supporting the residue assignment for IiMDH; relaxation analysis of IiMDH proline-Cδ sites; NMR spectra of isolated [13Cδ,15N,2Hβγ4]-Pro (PDF)","language":[{"iso":"eng"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"type":"journal_article","article_type":"original","year":"2026","oa_version":"Published Version","_id":"23173","oa":1,"date_published":"2026-10-13T00:00:00Z","fulldoi":"https://doi.org/10.1021/acschembio.6c00587","corr_author":"1","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","publication_identifier":{"eissn":["1554-8937"],"issn":["1554-8929"]},"publication":"ACS Chemical Biology","day":"13","title":"Chemoenzymatic proline isotope labeling for solution and magic-angle spinning protein nuclear magnetic resonance"}