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Article

Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations.

Nature structural biology - 1 Nov 1997

Luo Y, Kay M S, Baldwin R L

Abstract excerpt

The apomyoglobin pH 4 folding intermediate contains the A, G, and H helices of myoglobin. Helix destabilizing mutations in the A and G helices are used to test whether the pH 4 folding intermediate of apomyoglobin folds cooperatively. Single glycine or proline mutations destabilize the intermediate substantially, showing that intrinsic helix propensities are important for stability of the intermediate. The A and...

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Identifiers

PMID: 9360609
DOI: 10.1038/nsb1197-925

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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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