Oxidative folding of peptides and proteins
With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides, The formation of disulfide bonds is probably the most influential modification of peptides and proteins. An elaborate set of cellular machinery exists to cata...
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| Other Authors: | , , |
| Format: | eBook |
| Language: | English |
| Published: |
Cambridge
Royal Society of Chemistry
2008
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| Series: | RSC Biomolecular sciences
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| Online Access: | |
| Collection: | RSC eBook Collection 1968-2009 - Collection details see MPG.ReNa |
Table of Contents:
- Preface. Foreword. Chapter 1. Oxidative Folding of Proteins in Vivo: Thioredoxins and the regulation of redox conditions in prokaryotes
- Dsb A B
- Eucaryotic PDIs
- Structure of Ero1/oxidation in the ER
- Oxidative folding in the ER
- Oxidative protein folding in mitochondria
- Cellular responses to redox stress
- Harnessing disulfide bond formation in the periplasm of bacteria for recombinant protein production. Chapter 2. Oxidative Folding of Proteins in vitro: The role of disulfide bonds for folding and stability of proteins
- Strategies for the oxidative refolding of disulfide-bonded proteins. Chapter 3. Redox potentials of cysteine residues in peptides and proteins: Methods for their determination. Chapter 4. Engineering disulfide bonds. Chapter 5. Selenocysteine as a probe of oxidative protein folding. Chapter 6. Oxidative Folding of Peptides in vitro: Oxidative folding of single-stranded disulfide-rich Peptides
- Regioselective disulfide formation
- Folding motifs of cysteine-rich peptides
- Double-stranded cysteine-peptides
- Multiple-strand cysteine-peptides. Chapter 7. Cysteine-based scaffolds for functional miniature proteins. Chapter 8. Selenocystine-peptides - Synthesis, folding and applications