![]() The revelation in 1989 that organellar chaperonins are proteinfolding machines prompted an immediate search for such machines in other compartments and kingdoms of life, resulting in the discovery in archaebacteria and, through homology, in the eukaryotic cytosol of additional double ring machines that mediate protein folding. This chapter continues with the subject of chaperonin-mediated protein folding, dealing with a second family of chaperonins found in archaebacteria and the eukaryotic cytosol, termed type II chaperonins. Readership: Cell and molecular biologists, biochemists and biophysicists, nanoscientists. Structural Insights into Hsp90 Function (Elaine Kirschke, Daniel Elnatan, Kliment Verba and David A Agard).Structure and Mechanism of AAA+ Chaperones (Shannon M Doyle, Andrea N Kravats and Sue Wickner).The Family of Small Heat Shock Proteins: Assembly and Binding Functions (C Slingsby and A R Clark).Structural Analysis of Type II Chaperonins in Archaebacteria and the Eukaryotic Cytosol (Arthur L Howrich).Structural Analysis of GroEL/GroES Chaperone-Mediated Protein Folding (Arthur L Howrich).Hsp70 Molecular Chaperones: Versatile Modular Nanomachines that Mediate Multiple Biological Functions (Lila M Gierasch). ![]() The beauty of what Mother Nature has devised to accomplish essential assisting actions for proteins in vivo is fully appreciable.Ĭhapter 1: Hsp70 Molecular Chaperones: Versatile Modular Nanomachines that Mediate Multiple Biological Functions (502 KB) 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. 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. 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.
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