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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.
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