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Article

Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme.

The Biochemical journal - 1 Jun 1993

Kanaya E, Ishihara K, Tsunasawa S, Nokihara K, Kikuchi M

Abstract excerpt

Lysozyme has two distinct folding domains, and in most molecules the alpha-helical domain folds more quickly than the beta-sheet domain in vitro [Radford, Dobson and Evans (1992) Nature (London) 358, 302-307]. In order to investigate the relationship between the formation of disulphide bonds and protein folding in vivo, we carried out cysteine scanning mutagenesis to shift positions of the disulphide bonds in...

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Identifiers

PMID: 8503881
DOI: 10.1042/bj2920469
PMCID: PMC1134233

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Source receipt: pubmed, retrieved 7 Sept 2026.

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