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Article

Effects of amino acid replacements on the reductive unfolding kinetics of pancreatic trypsin inhibitor.

Biochemistry - 8 Feb 1994

Mendoza J A, Jarstfer M B, Goldenberg D P

Abstract excerpt

In order to characterize the major transition states in the disulfide-coupled folding pathway of bovine pancreatic trypsin inhibitor (BPTI), the reductive unfolding kinetics of wild-type BPTI and 18 variants with single amino acid replacements were measured in the presence of varying concentrations of dithiothreitol (DTTSHSH). As observed previously for the wild-type protein, unfolding of the mutant proteins was...

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PMID: 7509189
DOI: 10.1021/bi00171a013

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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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