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Article

Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.

Chembiochem : a European journal of chemical biology - 1 Sept 2005

Collins Emily S, Wirmer Julia, Hirai Kenichi, Tachibana Hideki, Segawa Shin-ichi, Dobson Christopher M, Schwalbe Harald

Abstract excerpt

This report describes NMR-spectroscopic investigations of the conformational dynamics of disulfide bonds in hen-egg-white lysozyme substitution mutants. The following four systems have been investigated: 2SS(alpha), a lysozyme variant that contains C64A, C76A, C80A and C94A substitutions, was studied in water at pH 2 and 3.8 and in urea (8 M, pH 2); 2SS(beta) lysozyme, which has C6S, C30A, C115A and C127A...

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PMID: 16138305
DOI: 10.1002/cbic.200500196

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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