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Article

Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments.

Protein engineering - 1 Nov 2001

Ohkuri T, Ueda T, Tsurumaru M, Imoto T

Abstract excerpt

We prepared two dissected fragments of hen lysozyme and examined whether or not these two fragments associated to form a native-like structure. One (Fragment I) is the peptide fragment Asn59-homoserine-105 containing Cys64-Cys80 and Cys76-Cys94. The other (Fragment II) is the peptide fragment Lys1-homoserine-58 connected by two disulfide bridges, Cys6-Cys127 and Cys30-Cys115, to the peptide fragment...

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Identifiers

PMID: 11742101
DOI: 10.1093/protein/14.11.829

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments.PMID 11742101Read ↗

Analysis of the early stage of the folding process of reduced lysozyme using all lysozyme variants containing a pair of cysteines.Semantic proximity Read ↗

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NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.Semantic proximity Read ↗

Analyses of native disulfide bond formations in the early stage of the folding process in mutant lysozymes where the long-range interactions in the denatured state were modulated.Semantic proximity Read ↗

Effect of W62G mutation of hen lysozyme on the folding in vivo.Semantic proximity Read ↗

Propensities for the formation of individual disulfide bonds in hen lysozyme and in the size and stability of disulfide-associated submolecular structures.Semantic proximity Read ↗

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