Polyteknisk Boghandel

The formation of disulfide bonds is probably the most influential modification of peptides and proteins with significant progress achieved in recent years, both concerning their in vivo situation and in vitro manipulation.

This book is the first monograph covering this exciting and rapidly developing area with contributions from major experts in the field providing a comprehensive overview.

The topics covered include the enzymes involved in the correct oxidative folding of cysteine-containing proteins in prokaryotes and eukaryotes, their mimicking for successful in vitro folding of proteins, including synthetic replicates and important aspects concerning cysteine-rich peptides.

The book will be particularly valuable for peptide and protein chemists involved in related research and production.

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.