The mitochondrial permeability transition (PT) is a permeability increase of the inner
mitochondrial membrane mediated by a channel, the permeability transition pore (PTP) …

The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …

A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

Protein functions are dynamically regulated by allostery, which enables conformational
communication even between faraway residues, and expresses itself in many forms, akin to …

The heat shock protein (Hsp) 90 chaperone machinery regulates the activity of hundreds of
client proteins in the eukaryotic cytosol. It undergoes large conformational changes between …

Large-scale conformational changes are essential to link protein structures with their
function at the cell and organism scale, but have been elusive both experimentally and …

The concept of allostery has become a central tenet in the study of biological systems. In
parallel, the discovery of allosteric drugs is generating new opportunities to selectively …

While structural symmetry is a prevailing feature of homo-oligomeric proteins, asymmetry
provides unique mechanistic opportunities. We present the crystal structure of full-length …

TRAP1 is the mitochondrial paralog of the heat shock protein 90 (HSP90) chaperone family.
Its activity as an energy metabolism regulator has important implications in cancer …

Molecular chaperones HSP90 and HSP70 are essential regulators of the folding and
activation of a disparate ensemble of client proteins. They function through ATP hydrolysis …