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6 January 2014

978 0 85404 148 0
Royal Society of Chemistry
GBP 119.95

Oxidative Folding of Peptides and Proteins (RSC Biomolecular Sciences)

J. Buchner and L. Moroder (eds)

The formation of disulfide bonds is one of the key post-translational modifications in proteins, and understanding their formation is of great importance for a range of applications.

This monograph presents an overview of the formation of disulfide bonds with insights into mechanisms of protein and peptide folding, in vivo and in vitro. The chapters are independent of each other, allowing the readers to pick and choose according to their particular areas of interest.

Chapter 1 to 5 cover protein oxidative folding, whereas the remaining three chapters cover folding of cysteine-rich peptides. Chapter 1, focusing on oxidative folding in vivo, is split into eight sections, with the first two focusing on thioredoxins and the regulation of redox conditions, a topic I find particularly interesting, and disulfide bond formation in prokaryotes. Both sections present a review of the current state of knowledge. Chapter 1.3 takes a more practical approach by discussing the recombinant expression of proteins in Escherichia coli, and strategies for achieving correct oxidative folding and disulfide bond formation. Chapter 2 and its subsections describe oxidative folding in vitro. Chapters 6–8 make up about a third of the volume, and concentrate on the oxidative folding of peptides. I found Chapter 7 particularly interesting in its up-to-date review of the use of cysteine-containing peptides as scaffolds for protein mimics.

The chapters that stand out as particularly useful are Chapters 1.3, mentioned above, Chapter 3, which covers an in-depth method for determining redox potentials of cysteine residues, and Chapter 8, which covers applications for selenocysteine peptides. These three cover more practical advice, and therefore stand out from the other chapters, which are all more theoretical.

All chapters have illustrations, and protein structures are used when possible to highlight points made in the text. However, some of the structure images would benefit from higher resolutions.

The index is brief, but the chapter headings are descriptive, and finding what is of interest should not be difficult. The strengths of this book are also its weaknesses. Owing to the wide scope, each chapter is, by necessity, short and to the point, and does on occasion leave the reader wanting more. However, each chapter comes with an extensive list of references, for further reading, and the range of subjects introduces areas of oxidative folding the reader may have been unfamiliar with, but which may turn out to be useful for future work. I would suggest the target audience of this book is researchers with an interest in the field of oxidative folding and regulation of proteins, as well as postgraduate students looking to get a good overview of this varied field.

Mads Gabrielsen (Beatson Institute of Cancer Research, UK)

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