Folding of peptides and proteins: role of disulfide bonds, recent developments
Abstract: Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction. However, regulating or analyzing the structures of folding intermediates of peptides and proteins continues to be a difficult problem. Recently, the development of several techniques in peptide chemistry and biotechnology has resulted in the availability of some powerful tools for studying protein folding in the context of the structural analysis of native, mutant proteins, and folding intermediates. In this review, recent developments in the field of disulfide-coupled peptide and protein folding are discussed, from the viewpoint of chemical and biotechnological methods, such as analytical methods for the detection of disulfide pairings, chemical methods for disulfide bond formation between the defined Cys residues, and applications of diselenide bonds for the regulation of disulfide-coupled peptide and protein folding.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Folding of peptides and proteins: role of disulfide bonds, recent developments ; volume:4 ; number:6 ; year:2013 ; pages:597-604
Biomolecular concepts ; 4, Heft 6 (2013), 597-604
- Creator
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Hidaka, Yuji
Shimamoto, Shigeru
- DOI
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10.1515/bmc-2013-0022
- URN
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urn:nbn:de:101:1-2409241615328.663111411415
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:25 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Hidaka, Yuji
- Shimamoto, Shigeru
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