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Article

Structural studies of N-terminal mutants of connexin 32 using (1)H NMR spectroscopy.

Archives of biochemistry and biophysics - 1 Oct 2012

Kalmatsky B D, Batir Y, 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 functional connexin molecules contains a flexible turn around G12 (Arch. Biochem. Biophys.490:9,200...

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Identifiers

PMID: 22705201
DOI: 10.1016/j.abb.2012.05.027
PMCID: PMC3938314

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22705201-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

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

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