Proteins, in general, fold to a well-organized three-dimensional structure in order to function.
The stability of this functional shape can be perturbed by external environmental conditions …

The cytoplasm is an aqueous, highly crowded solution of active macromolecules. Its
properties influence the behavior of proteins, including their folding, motion, and …

Proteins from organisms that have adapted to environmental extremes provide attractive
systems to explore and determine the origins of protein stability. Improved hydrophobic core …

The complex, multidimensional energy landscape of biomolecules makes the extraction of
suitable, nonintuitive collective variables (CVs) that describe their conformational transitions …

Molecular mechanisms underlying the thermal response of cells remain elusive. On the
basis of the recent result that the short-time diffusive dynamics of the Escherichia coli …

Proteins from thermophilic organisms are stable and functional well above ambient
temperature. Understanding the molecular mechanism underlying such a resistance is of …

Comparing homologous enzymes adapted to different thermal environments aids to shed
light on their delicate stability/function trade-off. Protein mechanical rigidity was postulated to …

We present a novel multi-conformation Monte Carlo simulation method that enables the
modeling of protein–protein interactions and aggregation in crowded protein solutions. This …

Diffusion of a two component fluid is studied in the framework of differential equations, but
where these equations are systematically derived from a well-defined microscopic model …

Protein dynamics is a manifestation of the complex trajectories of these biomolecules on a
multidimensional rugged potential energy surface (PES) driven by thermal energy. At …