Structural studies of N-terminal mutants of Connexin 32 using 1H NMR spectroscopy

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Structural studies of the N-terminus of Connexin 32 using 1H NMR spectroscopy.

The amino terminus of gap junction proteins, connexins, plays a fundamental role in voltage gating and ion permeation. We have previously shown with (1)H NMR that the structure of the N-terminus of a representative connexin molecule contains a flexible turn around glycine 12 [P.E. Purnick, D.C. Benjamin, V.K. Verselis, T.A. Bargiello, T.L. Dowd, Arch. Biochem. Biophys. 381 (2000) 181-190] allow...

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ژورنال

عنوان ژورنال: Archives of Biochemistry and Biophysics

سال: 2012

ISSN: 0003-9861

DOI: 10.1016/j.abb.2012.05.027