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Article

Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of alphaB-crystallin.

Molecular and cellular biochemistry - 1 Apr 2001

Shroff N P, Bera S, Cherian-Shaw M, Abraham E C

Abstract excerpt

Amino acid residues 57-69 in alphaB-crystallin have been implicated as a target protein binding site. Moreover, a direct correlation between the extent of alpha-crystallin hydrophobicity and chaperone-like activity has been demonstrated. The purpose of this study was to mutate a moderately hydrophobic residue Met-68 (M-68) in the above region to strongly hydrophobic and hydrophilic residues and show whether...

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Source

Identifiers

PMID: 11451372
DOI: 10.1023/a:1010834107809

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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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