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Article

The role of cysteine oxidation in the thermal inactivation of T4 lysozyme.

Protein engineering - 1 Jan 2000

Perry L J, Wetzel R

Abstract excerpt

Wild-type T4 lysozyme contains unpaired cysteine residues at positions 54 and 97. To investigate the role these residues play in the thermal inactivation of the wild-type, we constructed a double mutant with these cysteines replaced with valine and serine. This molecule, T4 lysozyme (C54V/C97S), is more stable than the wild-type to inactivation at 70 degrees C at pH 6.5 and 8.0. Guanidine hydrochloride...

Topics

Amino Acid Sequence
Cysteine
Hot Temperature
Kinetics
Molecular Sequence Data
Molecular Structure
Muramidase
Mutation
Oxidation-Reduction
Protein Engineering
T-Phages

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PMID: 3507692
DOI: 10.1093/protein/1.2.101

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-3507692-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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