The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …

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

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

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 …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …

Coarse-grained models are emerging as a practical alternative to all-atom simulations for
the characterization of protein folding mechanisms over long time scales. While a decade …

In recent years significant effort has been devoted to exploring the potential effects of
macromolecular crowding on protein folding and association phenomena. Theoretical …

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 …

Nanoparticles (NPs) and other engineered nanomaterials have great potential as
nanodrugs or nanomedical devices for biomedical applications. However, the adsorption of …

The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate
substrates of GroEL share the (βα) 8 TIM-barrel fold, but how the chaperonin promotes …