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Relative effects of primary and tertiary structure on helix formation in myoglobin and alpha-lactalbumin


, : Relative effects of primary and tertiary structure on helix formation in myoglobin and alpha-lactalbumin. Biopolymers 10(5): 895-914

UV optical rotatary dispersion was used to study the degree of helicity in the CNBr peptides of myoglobin and reduced S-carboxymethylated alpha -lactalbumin in aqueous and ethanolic solutions. In aqueous solution the degree of helicity was small. In the native form, alpha -lactalbumin has lower % helix content than myoglobin. However, helix formation comparable to that in myoglobin peptides was induced by high ethanol concn. in the 33-residue C-terminal peptide of alpha -lactalbumin.

US$19.90

PMID: 5572633

DOI: 10.1002/bip.360100512


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