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Article

Effect of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures.

Biochemistry - 3 Apr 1990

Anderson W D, Fink A L, Perry L J, Wetzel R

Abstract excerpt

Equilibrium and kinetic effects on the folding of T4 lysozyme were investigated by fluorescence emission spectroscopy in cryosolvent. To study the role of disulfide cross-links in stability and folding, a comparison was made with a mutant containing an engineered disulfide bond between Cys-3 (Ile-3 in the wild type) and Cys-97, which links the C-terminal domain to the N terminus of the protein [Perry & Wetzel...

Topics

Cross-Linking Reagents
Disulfides
Kinetics
Muramidase
Mutation
Protein Conformation
Protein Denaturation
Protein Engineering
Spectrometry, Fluorescence
T-Phages
Temperature

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Tryptophan

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Identifiers

PMID: 2334694
DOI: 10.1021/bi00465a026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2334694-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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