Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Atomistic simulations play a central role in many fields of science. However, their usefulness
is often limited by the fact that many systems are characterized by several metastable states …

The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

Allosteric regulatory processes are implicated at all levels of biological function. Recent
advances in our understanding of the diverse and functionally significant class of intrinsically …

The OPEP coarse-grained protein model has been applied to a wide range of applications
since its first release 15 years ago. The model, which combines energetic and structural …

Linking cell signaling events to the fundamental physicochemical basis of the
conformational behavior of single molecules and ultimately to cellular function is a key …

Molecular Dynamics (MD) plays a fundamental role in characterizing protein disordered
states that are emerging as crucial actors in many biological processes. Here we assess the …

Orthosteric drugs block the active site to obstruct function; allosteric drugs modify the
population of the active state, to modulate function. Available data lead us to propose that …

The kinase-inducible domain interacting (KIX) domain is a highly conserved independently
folding three-helix bundle that serves as a docking site for transcription factors, whereupon …