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 …

BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular
chaperones, which perform numerous cellular functions that affect almost all aspects of the …

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

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

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 …

Abstract α-synuclein (αS) is an intrinsically disordered protein whose fibrillar aggregates are
the major constituents of Lewy bodies in Parkinson's disease. Although the specific function …

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 …