The traditional computational modeling of protein structure, dynamics, and interactions
remains difficult for many protein systems. It is mostly due to the size of protein …

A fundamental challenge in biological research is achieving an atomic-level description and
mechanistic understanding of the function of biomolecules. Techniques for biomolecular …

Intrinsically disordered proteins (IDPs) perform a broad range of functions in biology,
suggesting that the ability to design IDPs could help expand the repertoire of proteins with …

Many intrinsically disordered proteins (IDPs) may undergo liquid–liquid phase separation
(LLPS) and participate in the formation of membraneless organelles in the cell, thereby …

The formation and viscoelastic properties of condensates of intrinsically disordered proteins
(IDPs) is dictated by amino acid sequence and solution conditions. Because of the …

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 …

Molecular dynamics simulations hold the promise of providing an atomic-level description of
protein folding that cannot easily be obtained from experiments. Here, we examine the …

A new level of chromosome organization, topologically associating domains (TADs), was
recently uncovered by chromosome conformation capture (3C) techniques. To explore TAD …

Molecular dynamics simulations allow for atomic-level characterization of biomolecular
processes such as the conformational transitions associated with protein function. The …

We describe different Bayesian ensemble refinement methods, examine their interrelation,
and discuss their practical application. With ensemble refinement, the properties of dynamic …