The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …

The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by
sequestering nonnative polypeptides in a cage-like structure. Here we define the …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Chaperonins are large ring assemblies that assist protein folding to the native state by
binding nonnative proteins in their central cavities and then, upon binding ATP, release the …

GroEL and GroES form a chaperonin nano-cage for proteins up to∼ 60 kDa to fold in
isolation. Here we explored the structural features of the chaperonin cage critical for rapid …

The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by
actions of binding and encapsulation. ATP binding initiates a series of conformational …

The chaperonin-mediated folding reaction is an essential ATP-dependent reaction that
provides kinetic assistance to the process of protein folding to the native state in a variety of …

By virtue of their general ability to bind (hold) translocating or unfolding polypeptides
otherwise doomed to aggregate, molecular chaperones are commonly dubbed “holdases” …