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 …

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

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 …

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 …

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

Proteins are increasingly used in basic and applied biomedical research. Many proteins,
however, are only marginally stable and can be expressed in limited amounts, thus …

Abstract Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments
have been used to study chemical exchange processes in molecules since the early 1960s …

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