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Article

Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis.

Biochemistry - 30 Apr 1991

Hughson F M, Barrick D, Baldwin R L

Abstract excerpt

A partly folded form (I) of apomyoglobin has an alpha-helix content of about 35%; in an earlier study, hydrogen exchange revealed that the A, G, and H helices are folded, while much of the rest of the protein is not [Hughson, F. M., Wright, P. E., & Baldwin, R. L. (1990) Science 249, 1544-1548]. Because A, G, and H form a compact subdomain in native myoglobin, we proposed that nativelike packing interactions...

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Identifiers

PMID: 2021603
DOI: 10.1021/bi00231a001

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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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