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Article

Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange.

Journal of molecular biology - 27 Oct 1995

Clarke J, Hounslow A M, Fersht A R

Abstract excerpt

The hydrogen exchange behaviour of two stabilised disulfide mutants of barnase has been examined using NMR H/2H exchange measurements. The choice of experimental conditions is crucial in experiments to study the effects of mutations on local and global stability and dynamic behaviour of proteins. If exchange conditions allow both local and global unfolding events to be examined, then a comparison of three...

Topics

Bacillus
Bacterial Proteins
Disulfides
Enzyme Stability
Hydrogen
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Structure
Mutation
Protein Folding
Protein Structure, Secondary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ribonucleases

Thermodynamics

Source

Identifiers

PMID: 7473730
DOI: 10.1006/jmbi.1995.0569

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7473730-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange.PMID 7473730Read ↗

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A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.Semantic proximity Read ↗

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Dynamic spin label study of the barstar-barnase complex.Semantic proximity Read ↗

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