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Article

Stabilization of GroEL minichaperones by core and surface mutations.

Journal of molecular biology - 19 May 2000

Wang Q, Buckle A M, Fersht A R

Abstract excerpt

We report the crystal structures of two hexa-substituted mutants of a GroEL minichaperone that are more stable than wild-type by 7.0 and 6.1 kcal mol(-1). Their structures imply that the increased stability results from multiple factors including improved hydrophobic packing, optimised hydrogen bonding and favourable structural rearrangements. It is commonly believed that protein core residues are immutable and...

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Identifiers

PMID: 10801358
DOI: 10.1006/jmbi.2000.3716

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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