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Article

The stabilizing effects of hydrophobic cores on peptide folding of bovine-pancreatic-trypsin-inhibitor folding-intermediate model.

European journal of biochemistry - 15 Jul 1994

Kwon D Y

Abstract excerpt

A synthetic peptide model composed of alpha-helical and beta-sheet portions (P alpha P beta) is a crucial folding intermediate in the folding of bovine pancreatic trypsin inhibitor (BPTI), which contains 30 amino acid residues, and provides a good model for studying the folding structure. Using this model the roles of hydrophobic cores, such as non-polar amino acids and a short beta strand, in the folding...

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Identifiers

PMID: 7519984
DOI: 10.1111/j.1432-1033.1994.tb19035.x

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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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