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Article

Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.

Protein engineering - 1 Nov 1995

Uchiyama H, Perez-Prat E M, Watanabe K, Kumagai I, Kuwajima K

Abstract excerpt

Five mutant alpha-lactalbumins, with one or two amino acid substitution(s) in the B helix, were engineered to examine the relation between the stability of the molten globule state and the hydrophobicity of these amino acids. The mutation sites (Thr29, Ala30 and Thr33) have been chosen on the basis of comparison of the amino acid sequences of goat, bovine and gunea pig alpha-lactalbumin, in which the guinea pig...

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PMID: 8819981
DOI: 10.1093/protein/8.11.1153

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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