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Secondary Structure Analysis of a Functional Construct of Caveolin-1 Reveals a Long C-Terminal Helix

By Sarah M. Plucinsky and Kerney Jebrell Glover

Abstract

AbstractCaveolin-1 is an integral membrane protein that is the primary component of cell membrane invaginations called caveolae. While caveolin-1 is known to participate in a myriad of vital cellular processes, structural data on caveolin-1 of any kind is severely limited. In order to rectify this dearth, secondary structure analysis of a functional construct of caveolin-1, containing the intact C-terminal domain, was performed using NMR spectroscopy in lyso-myristoylphosphatidylglycerol micelles. Complete backbone assignments of caveolin-1 (residues 62–178) were made, and it was determined that residues 62–79 were dynamic; residues 89–107, 111–128, and 132–175 were helical; and residues 80–88, 108–110, and 129–131 represent unstructured breaks between the helices

Publisher: Biophysical Society. Published by Elsevier Inc.
Year: 2015
DOI identifier: 10.1016/j.bpj.2015.08.030
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