{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T11:59:40Z","timestamp":1777982380019,"version":"3.51.4"},"reference-count":39,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T00:00:00Z","timestamp":1771286400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T00:00:00Z","timestamp":1771286400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR\u201020\u2010CE29\u20100015\u201001"],"award-info":[{"award-number":["ANR\u201020\u2010CE29\u20100015\u201001"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Angew Chem Int Ed"],"published-print":{"date-parts":[[2026,3,23]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Insight into the conformational dynamics of proteins is essential toward understanding their function at a molecular level. The motions experienced by individual atoms in the protein can be precisely quantified through NMR relaxation rates, but their measurement requires well\u2010resolved spectral responses. Two\u2010dimensional\n                    <jats:sup>1<\/jats:sup>\n                    H\u2010\n                    <jats:sup>15<\/jats:sup>\n                    N correlation spectra are the standard approach to resolve amide signals in protein NMR, but come with an excessive cost in experimental time when spectra are heavily congested due to limited\n                    <jats:sup>15<\/jats:sup>\n                    N chemical shift dispersions. This limitation often thwarts the characterization of dynamics for intrinsically disordered proteins, especially when they feature low\u2010complexity or homopolymer regions, or short sample life\u2010times. Here, we introduce a fast, ultra\u2010selective\n                    <jats:sup>1<\/jats:sup>\n                    H\u2010\n                    <jats:sup>15<\/jats:sup>\n                    N 1D NMR method that allows high\u2010quality measurement of individual\n                    <jats:sup>15<\/jats:sup>\n                    N spin\u2010relaxation constants, even when\n                    <jats:sup>15<\/jats:sup>\n                    N resonances are merely 6\u20138\u00a0Hz apart. We demonstrate the new experiment by characterizing, for the first time, pico\u2010 to nanosecond dynamics along a 16\u2010residue polyglutamine stretch within the protein huntingtin, the causal agent of Huntington's disease, as well as millisecond conformational exchange in the SH3GL3 protein. The new experiment will find wide application in the study of conformational dynamics of intrinsically disordered proteins or any other biomacromolecule that features highly dense\n                    <jats:sup>1<\/jats:sup>\n                    H\u2010\n                    <jats:sup>15<\/jats:sup>\n                    N 2D spectra.\n                  <\/jats:p>","DOI":"10.1002\/anie.202519206","type":"journal-article","created":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T05:33:36Z","timestamp":1771392816000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Fast Ultra\u2010Selective\n                    <sup>1<\/sup>\n                    H\u2010\n                    <sup>15<\/sup>\n                    N 1D NMR Spectroscopy Unlocks Atom\u2010Resolved Dynamics of Low\u2010Complexity Protein Regions"],"prefix":"10.1002","volume":"65","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-2115-3804","authenticated-orcid":false,"given":"Wiktor","family":"Adamski","sequence":"first","affiliation":[{"name":"CNRS, Univ. 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Lille, Institut Pasteur de Lille UMR\u00a09031 \u2013 Integrative Structural Biology Lille France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2556-5895","authenticated-orcid":false,"given":"Davy","family":"Sinnaeve","sequence":"additional","affiliation":[{"name":"CNRS, Univ. Lille, Institut Pasteur de Lille UMR\u00a09031 \u2013 Integrative Structural Biology Lille 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