Protein Misassembly

Overview

The role that primary amino acid sequences plays in influencing the partitioning of polypeptides between productive folding and irreversible aggregation pathways has introduced a whole new dimension to the folding problem. The volume deals with the structures of the products of protein misassembly and the role of amino acid sequences in favoring these structures.

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Overview

The role that primary amino acid sequences plays in influencing the partitioning of polypeptides between productive folding and irreversible aggregation pathways has introduced a whole new dimension to the folding problem. The volume deals with the structures of the products of protein misassembly and the role of amino acid sequences in favoring these structures.

Audience: Molecular biologists, biochemists, immunologists, and biophysicists.

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Editorial Reviews

Doody's Review Service
Reviewer: Gene A. Homandberg, PhD (Rush Medical College of Rush University)
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.
From the Publisher
"The authority, originality, and editing of the reviews are first class."
—NATURE
"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists."
—JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
"...this book provides a revealing and up-to-date look at many aspects of protein aggregation and amyloid fibril formation...will be invaluable for anyone, and especially newcomers interested in the structure of amyloid and its molecular basis."
—Anthony L. Fink, Ph.D., University of California, Santa Cruz, in AMYLOID (1999)
From The Critics
Reviewer: Gene A. Homandberg, PhD(Rush Medical College of Rush University)
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.
Gene A. Homandberg
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. 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. 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. 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. This book is highly recommended for advanced protein chemists, and molecular or cell biologists who need a better understanding of both how protein foldingcan go awry and of the consequences of these alternative folding pathways on protein function.

3 Stars from Doody
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Product Details

  • ISBN-13: 9780120342501
  • Publisher: Elsevier Science
  • Publication date: 10/22/1997
  • Edition number: 1
  • Pages: 282

Table of Contents

R. Jaenicke and R. Seckler, Protein Misassembly in Vitro.
M.P. Schlunegger, M.J. Bennett, and D. Eisenberg, Oligomer Formation by 3D Domain Swapping: A Model for Protein Assembly and Misassembly.
M. Sunde and C. Blake, The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction.
W. Colon, Z. Lai, H.A. Lashuel, J. McCulloch, S.L. McCutchen, G.J. Miroy, S.A. Peterson, and J.W. Kelly, Transthyretin Quaternary and Tertiary Structural Changes Facilitate Misassembly into Amyloid.
R. Wetzel, Domain Stability in Immunoglobulin Light Chain Deposition Disorders.
S. Betts, C. Haase-pettingel, and J. King, Mutational Effects on Inclusion Body Formation.
Author Index.
Subject Index.

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