The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

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 …

Biological molecules are often highly dynamic, and this flexibility can be critical for function.
The large range of sampled timescales and the fact that many of the conformers that are …

A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …

The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in
cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE …

Protein folding in the cell requires ATP-driven chaperone machines such as the conserved
Hsp70 and Hsp90. It is enigmatic how these machines fold proteins. Here, we show that …

Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes
including protein synthesis, membrane translocation, and folding. We used nuclear …

The proposal that coupled folding to binding is not an obligatory mechanism for intrinsically
disordered (ID) proteins was put forward 10 years ago. The notion of fuzziness implies that …