Biophysics Of Molecular Chaperones

Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

The proteome consists of a complex mixture of proteins each of which need to be folded correctly in order to function for the health of the organism, and many of these proteins require molecular chaperones to reach the correct conformation and, in some cases, to remain in a folded form. In Molecular Chaperones: Methods and Protocols, expert researchers address a wide variety of approaches to the study these mechanisms, featuring the workings of heat shock proteins and heat shock transcription factors, in vitro and in vivo. Written in the highly successful Methods in Molecular BiologyTM series format, chapters features introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Molecular Chaperones: Methods and Protocols serves as an ideal guide for all scientists who wish to pursue this vital biological action and its impact on human health and disease.

Molecular Chaperones in Human Disorders, Volume 114 in the Advances in Protein Chemistry and Structural Biology series, provides an overview of current developments in mechanisms underlying DNA repair and their involvement in maintaining chromatin repair, the balance between chromosomal repair pathways, tumorigenesis, immune signaling and infection-induced inflammation. Chapters in this new release cover Functional principles and regulation of molecular chaperones, Chaperones and retinal disorders, Protein misfolding and degradation in genetic diseases, Chaperone dysfunction in hereditary myopathic diseases, Diseases caused by functional disorder of molecular chaperones residing in the endoplasmic reticulum, and many other timely topics. Describes advances in our understanding on DNA repair mechanisms and the involvement of their dysregulation in promoting diseases Provides an ideal resource for a very wide audience of specialists, researchers and students Contains timely chapters written by well-renown authorities in their field Presents information that is well supported by a number of high quality illustrations, figures and tables

Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?, by A. Katrine Wallis and Robert B. Freedman Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins, by Cordelia Schiene-Fischer, Tobias Aumüller and Gunter Fischer Small Heat-Shock Proteins: Paramedics of the Cell, by Gillian R. Hilton, Hadi Lioe, Florian Stengel, Andrew J. Baldwin und Justin L. P. Benesch Allostery in the Hsp70 Chaperone Proteins, by Erik R. P. Zuiderweg, Eric B. Bertelsen, Aikaterini Rousaki, Matthias P. Mayer, Jason E. Gestwicki and Atta Ahmad Hsp90: Structure and Function, by Sophie E. Jackson Extracellular Chaperones, by Rebecca A. Dabbs, Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd and Mark R. Wilson

Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective. ​

This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology – more specifically, in protein folding pathways.

This second edition volume expands on the previous edition with new discussions on the latest techniques used to study molecular chaperones and the stress response. The chapters in this book cover such as analysis of the initiation and regulation of the stress response; the role of heat shock protein 90 (Hsp90) in gene expression through chromosome-immunoprecipitation; features of chaperone function and biology; the emerging role of the extracellular HSPs; and the use of chaperones as biomarkers. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting-edge and thorough, Chaperones: Methods and Protocols, Second Edition is a valuable resource for all researchers who want to learn more about this interesting and developing field.