Description
Book SynopsisThis 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.
Table of ContentsHsp70 Molecular Chaperones: Versatile Modular Nanomachines that Mediate Multiple Biological Functions (Lila M Gierasch); Structural Analysis of GroEL/GroES Chaperone-mediated Protein Folding (Arthur L Howrich); Structural Analysis of Type II Chaperonins in Archaebacteria and the Eukaryotic Cytosol (Arthur L Howrich); The Small Heat Shock Proteins Family: Assembly and Binding Functions (C Slingsby & A R Clark); Structure and Mechanism of AAA+ Chaperones (Shannon M Doyle, Andrea N Kravats & Sue Wickner); Hsp90 ATP-dependent Molecular Chaperones (David Agard);
