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Article

Alpha-helix stability and the native state of myoglobin.

Biochemistry - 30 Nov 1993

Lin L, Pinker R J, Kallenbach N R

Abstract excerpt

Native proteins fold to form structures that contain secondary-structure regular patterns in the peptide backbone, such as alpha-helix, beta-structure, and turns with high frequency. The role of this secondary structure in stabilizing the native folded state is presently unclear. Alanine substitutions at helical sites in myoglobin show no correlation with the helical propensity of the side chains involved. In an...

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Identifiers

PMID: 8251481
DOI: 10.1021/bi00210a011

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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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