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Article

The mutation Asp69-->Ser affects the chaperone-like activity of alpha A-crystallin.

European journal of biochemistry - 15 Sept 1995

Smulders R H, Merck K B, Aendekerk J, Horwitz J, Takemoto L, Slingsby C, Bloemendal H, De Jong W W

Abstract excerpt

alpha-Crystallins are members of the family of small heat-shock proteins. The conformation and mode of action of these 'junior chaperones' are unknown. To investigate the structure and chaperone-like activity, four mutants of bovine alpha A-crystallin were generated by site-directed mutagenesis. In comparison with wild-type alpha A-crystallin, the D69S mutant, in which a highly conserved charged residue has been...

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Identifiers

PMID: 7588723
DOI: 10.1111/j.1432-1033.1995.834zz.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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