Overview of the Regulation of Disulfide Bond Formation in Peptide and Protein Folding

Yuji Hidaka1

1 Faculty of Science and Engineering, Kinki University, Higashi‐Osaka, Osaka
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 28.6
DOI:  10.1002/0471140864.ps2806s76
Online Posting Date:  April, 2014
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Disulfide bonds play a critical role in the maintenance of the native conformation of proteins under thermodynamic control. In general, disulfide bond formation is associated with protein folding, and this restricts the formation of folding intermediates such as misbridged disulfide isomers or kinetically trapped conformations, which provide important information related to how proteins fold into their native conformation. Therefore, numerous studies have focused on the structural analysis of folding intermediates in vitro. However, isolating or trapping folding intermediates, as well as the entire proteins, including mutant proteins, is not an easy task. Several chemical methods have recently been developed for examining peptide and protein folding and for producing, e.g., intact, post‐translationally modified, or kinetically trapped proteins, or proteins with misbridged disulfide bonds. This overview introduces chemical methods for regulating the formation of disulfide bonds of peptides and proteins in the context of the thermodynamic and kinetic control of peptide and protein folding. Curr. Protoc. Protein Sci. 76:28.6.1‐28.6.6. © 2014 by John Wiley & Sons, Inc.

Keywords: disulfide; folding; intermediate; kinetic; regioselective

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Table of Contents

  • Introduction
  • Preparation of Intact Peptides and Proteins
  • Regulation of Peptide and Protein Conformation by the Stepwise Formation of Disulfide Bonds
  • Regulation of Disulfide‐Coupled Peptide and Protein Folding by Chemical Additives
  • Conclusion
  • Literature Cited
PDF or HTML at Wiley Online Library


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Literature Cited

Literature Cited
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