{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T10:10:02Z","timestamp":1790071802761,"version":"4.0.1"},"reference-count":110,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:00:00Z","timestamp":1790035200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:00:00Z","timestamp":1790035200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000062","name":"National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"abstract":"<jats:p>Intrinsically disordered proteins (IDPs) are often readily characterized as soluble monomers, whereas their biological and pathological roles frequently involve transient, heterogeneous, or sparsely populated oligomers. Such assemblies are often described as \u2018invisible\u2019 but invisibility is method\u2010dependent: Oligomers that escape direct detection by one technique may remain accessible through indirect or complementary measurements. Solution NMR is uniquely positioned to exploit exchange between observable monomers and NMR\u2010invisible oligomers, providing residue\u2010specific information on populations, kinetics, and intermolecular contacts. Other methods report on mass, stoichiometry, dimensions, morphology, or site\u2010specific distance distributions. Here, we discuss how integrating orthogonal measurements can overcome method\u2010specific blind spots and yield a self\u2010consistent model that simultaneously accounts for structure, populations, exchange kinetics, and morphology, something no single method can provide.<\/jats:p>","DOI":"10.1002\/1873-3468.70474","type":"journal-article","created":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T09:38:19Z","timestamp":1790069899000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Invisible but not inaccessible\u2014Revealing transient oligomers formed by intrinsically disordered proteins with solution\n                    <scp>NMR<\/scp>\n                    and complementary methods"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6412-805X","authenticated-orcid":false,"given":"Martin D.","family":"Gelenter","sequence":"first","affiliation":[{"name":"Laboratory of Chemical Physics National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health  Bethesda MD USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9809-5700","authenticated-orcid":false,"given":"Ad","family":"Bax","sequence":"additional","affiliation":[{"name":"Laboratory of Chemical Physics National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health  Bethesda MD USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,22]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"crossref","first-page":"9331","DOI":"10.1021\/acs.chemrev.1c01023","article-title":"NMR provides unique insight into the functional dynamics and interactions of intrinsically disordered proteins","volume":"122","author":"Camacho\u2010Zarco AR","year":"2022","journal-title":"Chem 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