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Article

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

Archives of biochemistry and biophysics - 1 Oct 2009

Kalmatsky B D, Bhagan S, Tang Q, Bargiello T A, Dowd T L

Abstract excerpt

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. B...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19638273
DOI: 10.1016/j.abb.2009.07.015
PMCID: PMC4510928

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-19638273-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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