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Article

Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by alphaA-crystallin.

The Journal of biological chemistry - 25 Oct 2002

Mchaourab Hassane S, Dodson Erich K, Koteiche Hanane A

Abstract excerpt

To elucidate the mechanism of alphaA-crystallin chaperone function, a detailed thermodynamic analysis of its binding to destabilized, site-directed mutants of T4 lysozyme was carried out. The selected mutants form a ladder of stabilities spanning the 5-10 kcal/mol range of free energy of unfolding. The crystal structures of the majority of the mutants have been previously determined and found to be similar to...

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Identifiers

PMID: 12189146
DOI: 10.1074/jbc.M206250200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by alphaA-crystallin.PMID 12189146Read ↗

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