{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T14:10:40Z","timestamp":1789567840420,"version":"build-2803163510"},"reference-count":41,"publisher":"American Chemical Society (ACS)","issue":"36","license":[{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100004795","name":"Institut Universitaire de France","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004795","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Protein dynamics is intimately coupled to hydration and stability, yet direct observation of the full sequence of thermally induced transitions remains instrumentally challenging. Here, we present a study that exploits the unique properties of Yfh1, one of the few natural proteins that undergoes both cold and heat denaturation at experimentally accessible temperatures, to probe protein dynamics by advanced elastic incoherent neutron-scattering instrumentation that allows detection of motions over an unprecedently broad momentum-transfer range and a range of 100\u2013330 K temperatures. We identified three distinct dynamical regimes, corresponding to the protein dynamical transition, cold denaturation, and heat denaturation. We could distinguish motions associated predominantly with the protein from those of its hydration shell. Importantly, our work also provides what is, to our knowledge, the first direct neutron-scattering observation of the dynamical consequences of cold denaturation in a protein. Hydration water displays a marked anomaly near 260 K that disappears following heat denaturation, revealing a strong coupling between native protein structure and water dynamics. These results establish a unified dynamical picture of protein stability across its complete thermal landscape.<\/jats:p>","DOI":"10.1021\/jacs.6c15050","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T17:05:23Z","timestamp":1788455123000},"page":"39307-39315","source":"Crossref","is-referenced-by-count":0,"title":["Following\nthe Complete Thermal Landscape of a Protein\nby Neutron Scattering"],"prefix":"10.1021","volume":"148","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5151-7710","authenticated-orcid":true,"given":"J.","family":"Peters","sequence":"first","affiliation":[{"name":"Universite\u0301 Grenoble Alpes , , ,","place":["Grenoble, France, 38400"]},{"name":"Spectroscopy Group, Institut Laue Langevin , ,","place":["Grenoble, France, 38042"]},{"name":"Institut Universitaire de France , ,","place":["Paris, France, 75231"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F.","family":"Turbant","sequence":"additional","affiliation":[{"name":"Universite\u0301 Grenoble Alpes , , ,","place":["Grenoble, France, 38400"]},{"name":"Spectroscopy Group, Institut Laue Langevin , ,","place":["Grenoble, France, 38042"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3047-654X","authenticated-orcid":true,"given":"A.","family":"Pastore","sequence":"additional","affiliation":[{"name":"Universite\u0301 Grenoble Alpes , , ,","place":["Grenoble, France, 38400"]},{"name":"The Wohl Institute, King\u2019s College London , ,","place":["London, U.K., SE59RT"]},{"name":"Elettra Sincrotrone Trieste , Basovizza, ,","place":["Trieste, Italy, 34149"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,2]]},"reference":[{"key":"2026091609131012600_cit1","first-page":"95","article-title":"Protein\nDynamics and Function","volume-title":"Protein Dynamics, Function,\nand Design","author":"Frauenfelder"},{"key":"2026091609131012600_cit2","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1038\/nature06522","article-title":"Dynamic personalities of proteins","volume":"450","author":"Henzler-Wildman","year":"2007","journal-title":"Nature"},{"issue":"5471","key":"2026091609131012600_cit3","doi-asserted-by":"publisher","first-page":"1604","DOI":"10.1126\/science.288.5471.1604","article-title":"How Soft Is\na Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering","volume":"288","author":"Zaccai","year":"2000","journal-title":"Science"},{"key":"2026091609131012600_cit4","doi-asserted-by":"publisher","DOI":"10.1017\/S0033583519000027","article-title":"Dynamics of proteins\nin solution","volume":"52","author":"Grimaldo","year":"2019","journal-title":"Q. Rev. Biophys."},{"issue":"4","key":"2026091609131012600_cit5","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1017\/S0033583502003840","article-title":"Protein dynamics studied by neutron\nscattering","volume":"35","author":"Gabel","year":"2002","journal-title":"Q. Rev. Biophys."},{"key":"2026091609131012600_cit6","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1088\/0034-4885\/39\/10\/001","article-title":"The study\nof biological structures by neutron scattering from solution, Rep","volume":"39","author":"Jacrot","year":"1976","journal-title":"Prog. 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