{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T23:50:45Z","timestamp":1791157845177,"version":"4.1.0"},"reference-count":57,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2015,1,24]],"date-time":"2015-01-24T00:00:00Z","timestamp":1422057600000},"content-version":"vor","delay-in-days":23,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["20934002"],"award-info":[{"award-number":["20934002"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2015,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Caveolin\u20101 is a main structural component of caveolae and essential for the invagination of caveolae by forming a hairpin\u2010shaped structure in the membrane\u2010inserting domain (residues, 102\u2013122). In this article, we determined the tertiary structures of the peptides comprising residues 93\u2013126 and 101\u2013126 of caveolin\u20101 in 1,1,1,3,3,3\u2010hexafluoro\u20102\u2010propanol (HFIP) aqueous solution and sodium dodecyl sulfate (SDS) micelles, respectively, by <jats:italic>nuclear magnetic resonance<\/jats:italic> (NMR) study. The self\u2010association of the peptides in SDS and dodecylphosphocholine (DPC) micelles was also studied by circular dichroism (CD), NMR, and sodium dodecyl sulfate\u2010polyacrylamide gel electrophoresis (SDS\u2010PAGE) techniques. Our results indicated that both peptides form a helix\u2013break\u2013helix structure with two helices spanning over Leu103\u2013Phe107 and Ile117\u2013His126 and a loop ranging over Gly108\u2013Gly116. The longer peptide 93\u2013126 showed a stronger propensity to aggregate than the shorter peptide 101\u2013126 in the micelles. Our results suggested that the glycine residues at positions 108 and 116 are important for the break of the helical structure of the membrane\u2010inserting domain and the segment Thr93\u2013Arg101 flanking the membrane\u2010inserting domain may play a role in the self\u2010association of the caveolin\u20101 protein at cellular membrane. \u00a9 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 11\u201320, 2015.<\/jats:p>","DOI":"10.1002\/bip.22597","type":"journal-article","created":{"date-parts":[[2014,12,5]],"date-time":"2014-12-05T12:13:59Z","timestamp":1417781639000},"page":"11-20","source":"Crossref","is-referenced-by-count":22,"title":["Structural study of caveolin\u20101 intramembrane domain by circular dichroism and nuclear magnetic resonance"],"prefix":"10.1002","volume":"104","author":[{"given":"Guanhua","family":"Yang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Supramolecular Structure and Materials Jilin University Changchun 130012 People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhe","family":"Dong","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Supramolecular Structure and Materials Jilin University Changchun 130012 People's Republic of 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