Overview
- This book discusses recent advances in understanding of the chaperonins and particularly multiple chaperonins
- The book covers evolution and possible modes of distribution of the multiple chaperonins, which is a novel topic on chaperonins
- Numerous halftones and line figures help the reader to understand and learn quickly
Part of the book series: Heat Shock Proteins (HESP, volume 11)
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Table of contents (10 chapters)
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Front Matter
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Structure–Function of Chaperonins
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Front Matter
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Multiple Chaperonins of Bacterial System
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Front Matter
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Multiple Chaperonins of Archaeal System
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Front Matter
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Evolution of Multiple Copies of Chaperonins
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Front Matter
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Keywords
About this book
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.
Editors and Affiliations
About the editors
C. M. Santosh Kumar started his research career as a molecular geneticist, exploring the functions of molecular chaperones in health and disease. His research aims at understanding the functions of the bacterial chaperonins, especially those of the multiple chaperonins. He has demonstrated that activity of a mycobacterial chaperonin is regulated by a phosphorylation switch that facilitates oligomerization. His current interests include unravelling the role of mycobacterial chaperonins in the establishment and progression of tubercular disease.
Shekhar C. Mande is a structural biologist interested in understanding the molecular attributes of mycobacterial stress proteins. He started his career as a structural biologist in understanding the structural features of peanut lectin. Further, he became interested in the structure-function relations of mycobacterial stress proteins, such as the redox proteins and heat-shock proteins. He led the way towards the understanding of structural features of the mycobacterial chaperonin proteins. His work demonstrated that mycobacterial chaperonins exhibit non-canonical attributes that are evolved to assist the pathogen in its disease establishment and progression. Concurrently, he began to explore the system wide functional interactions among the mycobacterial proteins. These investigations have led to the identification of several novel interactions that are currently being examined.
Bibliographic Information
Book Title: Prokaryotic Chaperonins
Book Subtitle: Multiple Copies and Multitude Functions
Editors: C. M. Santosh Kumar, Shekhar C. Mande
Series Title: Heat Shock Proteins
DOI: https://doi.org/10.1007/978-981-10-4651-3
Publisher: Springer Singapore
eBook Packages: Biomedical and Life Sciences, Biomedical and Life Sciences (R0)
Copyright Information: Springer Nature Singapore Pte Ltd. 2017
Hardcover ISBN: 978-981-10-4650-6Published: 14 September 2017
Softcover ISBN: 978-981-13-5191-4Published: 13 December 2018
eBook ISBN: 978-981-10-4651-3Published: 30 August 2017
Series ISSN: 1877-1246
Series E-ISSN: 1877-1254
Edition Number: 1
Number of Pages: IX, 170
Number of Illustrations: 8 b/w illustrations, 38 illustrations in colour
Topics: Protein Science, Microbiology, Biological and Medical Physics, Biophysics, Biomedical Engineering/Biotechnology, Cell Physiology