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Article

Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat.

Journal of molecular biology - 1 Dec 1995

Vogl T, Brengelmann R, Hinz H J, Scharf M, Lötzbeyer M, Engels J W

Abstract excerpt

The present differential scanning calorimetry and circular dichroism studies on the mechanism of protein stabilization by disulfide bonds were concerned with two questions: is the increase in unfolding entropy upon removal of disulfide links sufficient for the explantation of the general stability decrease of disulfide-deficient mutants? Is it immaterial by which residue cysteine residues are replaced when...

Topics

Calorimetry, Differential Scanning
Circular Dichroism
Cysteine
Disulfides
Enzyme Inhibitors
Models, Molecular
Mutation
Peptides
Protein Conformation
Protein Denaturation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thermodynamics

alpha-Amylases

Source

Identifiers

PMID: 7490764
DOI: 10.1006/jmbi.1995.0632

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7490764-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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