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 …

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 …

In theoretical modeling of a physical system, a crucial step consists of the identification of
those degrees of freedom that enable a synthetic yet informative representation of it. While in …

Understanding how local protein modifications, such as binding small-molecule ligands, can
trigger and regulate large-scale motions of large protein domains is a major open issue in …

The molecular chaperone HSP90 oversees the functional activation of a large number of
client proteins. Because of its role in multiple pathways linked to cancer and …

In this paper we investigate the structural and dynamical properties of the two major porins
(OmpF and OmpC) in Escherichia coli, using molecular dynamics (MD) simulations. In …

Elastic network models, simple structure-based representations of biomolecules where
atoms interact via short-range harmonic potentials, provide great insight into a molecule's …

Identifying dynamical, quasi-rigid domains in proteins provides a powerful means for
characterizing functionally oriented structural changes via a parsimonious set of degrees of …

Elastic network models ENMs allow to analytically predict the equilibrium dynamics of
proteins without the need of lengthy simulations and force fields, and they depend on a …

The ribosome is a very large complex that consists of many RNA and protein molecules and
plays a central role in protein biosynthesis in all organisms. Extensive interactions between …