On the substrate specificity of alpha-crystallin as a molecular chaperone.
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ABSTRACT: alpha-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by preventing the thermal aggregation of proteins. However, in contrast with many other heat shock proteins, alpha-crystallin fails to protect proteins from aggregation during refolding reactions. Our results indicate that alpha-crystallin has substrate specificity different from other chaperones and recognizes specific non-native intermediates formed on the denaturation pathway only, with no affinity for intermediates formed on the refolding pathway.
SUBMITTER: Das KP
PROVIDER: S-EPMC1136009 | biostudies-other | 1995 Oct
REPOSITORIES: biostudies-other
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