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Prokaryotic Chaperonins: Multiple Copies and Multitude Functions: Heat Shock Proteins, cartea 11

Editat de C. M. Santosh Kumar, Shekhar C. Mande
en Limba Engleză Hardback – 14 sep 2017
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. 
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Specificații

ISBN-13: 9789811046506
ISBN-10: 9811046506
Pagini: 170
Ilustrații: IX, 170 p. 46 illus., 38 illus. in color.
Dimensiuni: 155 x 235 mm
Ediția:1st ed. 2017
Editura: Springer Nature Singapore
Colecția Springer
Seria Heat Shock Proteins

Locul publicării:Singapore, Singapore

Cuprins

Chapter 1. Protein folding in the cell – the role of molecular chaperones.- Chapter 2.  Structure and function of the Hsp60 Chaperonins.-  Chapter 3. Classical View on the Regulation of Heat-shock response.- Chapter 4.  Recent Advances in the Regulation of Heat-shock Response- Chapter 5.   Multiple Chaperonins in Bacteria.- Chapter 6. Multiple Chaperonins in Mycobacteria.- Chapter 7.   Dynamic interplay of the Myxobacterial chaperonins.- Chapter 8.   Division of Labour in Rhizobial Chaperonins.- Chapter 9. Cooperativity of archaeal and bacterial chaperonins.- Chapter 10. Evolution of multiple chaperonins.

Notă biografică

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.


Textul de pe ultima copertă


​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. 

Caracteristici

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