Structure And Action Of Molecular Chaperones: Machines That Assist Protein Folding In The Cell
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A01=Arthur L Horwich
A01=Christine Slingsby
A01=David Agard
A01=Lila M Gierasch
A01=Sue Wickner
Author_Arthur L Horwich
Author_Christine Slingsby
Author_David Agard
Author_Lila M Gierasch
Author_Sue Wickner
Category=PSB
Category=PSD
Category=PSF
CCT/TRiC
CCTTRiC
Chaperones
Chaperonins
ClpA
ClpB
ClpX
DnaK
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GroEL
GroES
Heat Shock Proteins
Hsp100
Hsp60
Hsp70
Hsp90
Kinases
Nuclear Receptors
Polypeptide Binding
Protein Disaggregation
Protein Folding
Small Hsp
Thermosome
Product details
- ISBN 9789814749329
- Publication Date: 03 Oct 2016
- Publisher: World Scientific Publishing Co Pte Ltd
- Publication City/Country: SG
- Product Form: Hardback
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This unique volume reviews the beautiful architectures and varying mechanical actions of the set of specialized cellular proteins called molecular chaperones, which provide essential kinetic assistance to processes of protein folding and unfolding in the cell. Ranging from multisubunit ring-shaped chaperonin and Hsp100 machines that use their central cavities to bind and compartmentalize action on proteins, to machines that use other topologies of recognition — binding cellular proteins in an archway or at the surface of a "clamp" or at the surface of a globular assembly — the structures show us the ways and means the cell has devised to assist its major effectors, proteins, to reach and maintain their unique active forms, as well as, when required, to disrupt protein structure in order to remodel or degrade. Each type of chaperone is beautifully illustrated by X-ray and EM structure determinations at near- atomic level resolution and described by a leader in the study of the respective family. The beauty of what Mother Nature has devised to accomplish essential assisting actions for proteins in vivo is fully appreciable.
