The state-of-the-art for Monte Carlo (MC) simulations of biomacromolecules is reviewed.
Available methodologies for sampling conformational equilibria and associations of …

We review the role conformational ensembles can play in the analysis of biomolecular
dynamics, molecular recognition, and allostery. We introduce currently available methods for …

A new implicit solvation model for use in Monte Carlo simulations of polypeptides is
introduced. The model is termed ABSINTH for self‐Assembly of Biomolecules Studied by an …

Incorporation of effective backbone sampling into protein simulation and design is an
important step in increasing the accuracy of computational protein modeling. Recent …

Polyglutamine (poly (Q)) expansion is associated with protein aggregation into β-sheet
amyloid fibrils and neuronal cytotoxicity. In the mutant poly (Q) protein huntingtin, associated …

The loss of conformational entropy is a major contribution in the thermodynamics of protein
folding. However, accurate determination of the quantity has proven challenging. We …

Protein chains undergo conformational diffusion during folding and dynamics, experiencing
both thermal kicks and viscous drag. Recent experiments have shown that the …

Correlated motions in proteins can mediate fundamental biochemical processes such as
signal transduction and allostery. The mechanisms that underlie these processes remain …

It has been a long-standing conviction that a protein's native fold is selected from a vast
number of conformers by the optimal constellation of enthalpically favorable interactions. In …

The conformational entropy of proteins can make significant contributions to the free energy
of ligand binding. NMR spin relaxation enables site-specific investigation of conformational …