Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of
subunits presenting end cavities lined with hydrophobic binding sites for nonnative …

The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in
an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with …

The chaperonin ring assembly GroEL provides kinetic assistance to protein folding in the
cell by binding non-native protein in the hydrophobic central cavity of an open ring and …

Studies of protein-protein interactions, carried out in polymer solutions, are designed to
mimic the crowded environment inside living cells. It was shown that crowding enhances …

This chronologue seeks to document the discovery and development of an understanding of
oligomeric ring protein assemblies known as chaperonins that assist protein folding in the …

Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-
dependent movements that are coordinated in time and space owing to complex allosteric …

The GroEL/GroES chaperonin folding chamber is an encapsulated space of∼ 65Å diameter
with a hydrophilic wall, inside of which many cellular proteins reach the native state. The …

Abstract Characterization of transition and intermediate states of reactions provides insights
into their mechanisms and is often achieved through analysis of linear free energy …

Knowing the mechanism of allosteric switching is important for understanding how
molecular machines work. The CCT/TRiC chaperonin nanomachine undergoes ATP-driven …

Oxidative folding is the simultaneous process of forming disulphide bonds and native
structure in proteins. Pathways of oxidative folding are highly diverse and in eukaryotes are …