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Article

Partially formed native tertiary interactions in the A-state of cytochrome c.

Journal of molecular biology - 11 Jun 1999

Hostetter D R, Weatherly G T, Beasley J R, Bortone K, Cohen D S, Finger S A, Hardwidge P, Kakouras D S, Saunders A J, Trojak S K, Waldner J C, Pielak G J

Abstract excerpt

Considerable insight into protein structure, stability, and folding has been obtained from studies of non-native states. We have studied the extent of native tertiary contacts in one such molecule, the A-state of yeast iso-1-ferricytochrome c. Previously, we showed that the interface between the N and C-terminal helices is completely formed in the A-state. Here, we focus on interactions essential for forming the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10356334
DOI: 10.1006/jmbi.1999.2764

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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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