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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 t...

Topics

Amino Acid Sequence
Animals
Aprotinin
Cattle
Circular Dichroism
Hydrogen-Ion Concentration
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mutation
Protein Folding
Protein Structure, Secondary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7519984-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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The stabilizing effects of hydrophobic cores on peptide folding of bovine-pancreatic-trypsin-inhibitor folding-intermediate model.PMID 7519984Read ↗

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