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 …

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 …

The folding/misfolding and pharmacological rescue of multidomain ATP-binding cassette
(ABC) C-subfamily transporters, essential for organismal health, remain incompletely …

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 …

Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of
intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This …

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 …

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

Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …