Prokaryotic Chaperonins | Multiple Copies and Multitude Functions

C. M. Santosh Kumar (u. a.)

ISBN 10: 9811046506 / ISBN 13: 9789811046506

Published by Springer, 2017

About this Item

Prokaryotic Chaperonins | Multiple Copies and Multitude Functions | C. M. Santosh Kumar (u. a.) | Buch | Heat Shock Proteins | ix | Englisch | 2017 | Springer | EAN 9789811046506 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu Print on Demand.

Seller Inventory # 109797951

Bibliographic Details

• Title: Prokaryotic Chaperonins | Multiple Copies and Multitude Functions
• Publisher: Springer
• Publication Date: 2017
• Language: English
• ISBN 10: 9811046506
• ISBN 13: 9789811046506
• Binding: Buch
• Condition: Neu
• Dimensions: 241W x 160H x 15D millimeters 241 millimeters width by 160 millimeters height by 15 millimeters depth
• Weight: 474 grams
• Seller catalogs:
  • Bücher

About this title

Synopsis

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. 

About the Author

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.