Description: This Advances in Protein Chemistry volume on protein misassembly is an interesting addition to the series, with chapters on misassembly in vitro, oligomeric formation by 3d domain swapping, the structure of amyloid fibrils, domain stability in immunoglobulin light chain deposition disorders, and mutational effects on inclusion body formation.
Purpose: This volume is meant to present selected topics on these phenomena of alternative folded states, such as aggregates, which occur as integral parts of the energetic pathway for folding. Although this volume is a collection of several examples and therefore not comprehensive, the chapters do serve to provide a general description. However, a beginning overview chapter which separately reviews protein folding with examples and diagrams might have helped to attract the less advanced reader.
Audience: The reader is most likely to appreciate this book are protein chemists active in studies of protein folding, cell or molecular biologists with an interest in folding expressed proteins, and perhaps biomedical scientists with an interest in the role of protein misfolding in diseases, such as Alzheimer's disease.
Features: This attractive volume, with several color prints, has contributions by 19 authors, all experts in protein folding and conformation. At the front of the book is a tribute to the late C.B. Anfinsen, who, ironically, pioneered the concept that protein sequence dictates the nature of the folded state. This is a concept that has been greatly complicated by observations such as those included in this volume.
Assessment: This book is highly recommended for advanced protein chemists, and molecular or cell biologists who need a better understanding of both how protein folding can go awry and of the consequences of these alternative folding pathways on protein function.