Folding of small disulfide-rich proteins: clarifying the puzzle

The process by which small proteins fold to their native conformations has been intensively studied over the past few decades. The particular chemistry of disulfide-bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results th...

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Published inTrends in biochemical sciences (Amsterdam. Regular ed.) Vol. 31; no. 5; pp. 292 - 301
Main Authors Arolas, Joan L., Aviles, Francesc X., Chang, Jui-Yoa, Ventura, Salvador
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.05.2006
Subjects
Animals
Disulfides - chemistry
Models, Molecular
Oxidation-Reduction
Protein Conformation
Protein Folding
Proteins - chemistry
Proteins - metabolism
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Summary:The process by which small proteins fold to their native conformations has been intensively studied over the past few decades. The particular chemistry of disulfide-bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high level of diversity in folding mechanisms, differing in the heterogeneity and native disulfide-bond content of their intermediates. Information from folding studies of these proteins, together with the recent structural determinations of predominant intermediates, has provided new molecular insights into oxidative folding and clarifies the major rules that govern it.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2006.03.005