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Article

Paradoxical effects of substitution and deletion mutation of Arg56 on the structure and chaperone function of human alphaB-crystallin.

Biochemistry - 6 Feb 2007

Biswas Ashis, Goshe Jeffery, Miller Antonia, Santhoshkumar Puttur, Luckey Carol, Bhat Manjunatha B, Nagaraj Ram H

Abstract excerpt

Human alphaB-crystallin is a small heat-shock protein that functions as a molecular chaperone. Recent studies indicate that deletion of a peptide (54FLRAPSWF61) from its N-terminus makes it a better chaperone, and this particular sequence is thought to participate in substrate interaction and subunit exchange with alphaA-crystallin. To determine whether the positive charge on arginine 56 (R56) influences these...

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Identifiers

PMID: 17260942
DOI: 10.1021/bi061323w

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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