The traditional computational modeling of protein structure, dynamics, and interactions
remains difficult for many protein systems. It is mostly due to the size of protein …

The molecular details involved in the folding, dynamics, organization, and interaction of
proteins with other molecules are often difficult to assess by experimental techniques …

A unified coarse-grained model of three major classes of biological molecules—proteins,
nucleic acids, and polysaccharides—has been developed. It is based on the observations …

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 …

Allosteric interactions in the Hsp70 proteins are linked with their regulatory mechanisms and
cellular functions. Despite significant progress in structural and functional characterization of …

The ever increasing computer power, together with the improved accuracy of atomistic force
fields, enables researchers to investigate biological systems at the molecular level with …

Protein misfolding and aggregation are pathological events that place a significant amount
of stress on the maintenance of protein homeostasis (proteostasis). For prevention and …

The versatile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones
rely on allosteric interactions between their nucleotide-binding and substrate-binding …

Internal motions of folded proteins have been assumed to be ergodic, ie, that the dynamics
of a single protein molecule averaged over a very long time resembles that of an ensemble …

Molecular dynamics with coarse-grained models is nowadays extensively used to simulate
biomolecular systems at large time and size scales, compared to those accessible to all …