Proteins are macromolecules in perpetual motion, switching between structural states to
modulate their function. A detailed characterization of the precise yet complex relationship …

Background Structural excursions of a protein at equilibrium are key to biomolecular
recognition and function modulation. Protein modeling research is driven by the need to aid …

Controlling the quality of tertiary structures computed for a protein molecule remains a
central challenge in de-novo protein structure prediction. The rule of thumb is to generate as …

Proteins often undergo slow structural rearrangements that involve several angstroms and
surpass the nanosecond timescale. These spatiotemporal scales challenge physics-based …

More than fifty years of research in molecular biology have demonstrated that the ability of
small and large molecules to interact with one another and propagate the cellular processes …

Modeling structural transitions of a protein at equilibrium is central to understanding function
modulation but challenging due to the disparate spatio-temporal scales involved. Of …

We have long known that characterizing protein structures structure is key to understanding
protein function. Computational approaches have largely addressed a narrow formulation of …

The conformational space of proteins is complex and high dimensional, which makes its
analysis a highly challenging task. Understanding the structure and dynamics of proteins is …

To understand how proteins function on a cellular level, it is of paramount importance to
understand their structures and dynamics, including the conformational changes they …

The conformational space of proteins is complex and high dimensional, which makes its
analysis a highly challenging task. Understanding the structure and dynamics of proteins is …