Intrinsically disordered proteins and protein regions (IDRs) are abundant in eukaryotic
proteomes and play a wide variety of essential roles. Instead of folding into a stable …

Intrinsically disordered proteins (IDPs) exploit their plasticity to deploy a rich panoply of soft
interactions and binding phenomena. Advances in tailoring molecular simulations for IDPs …

Coacervation, or liquid-liquid phase separation (LLPS) of biomacromolecules, is
increasingly recognized to play an important role both intracellularly and in the extracellular …

Many proteins contain more than one folded domain, and such modular multi‐domain
proteins help expand the functional repertoire of proteins. Because of their larger size and …

Multidomain proteins with long flexible linkers and full-length intrinsically disordered
proteins (IDPs) are best defined as an ensemble of conformations rather than a single …

Conformations of polyampholytic intrinsically disordered proteins (IDPs) are controlled by
the interplay between Coulomb attractions of the opposite charges and long-range Coulomb …

Liquid–liquid phase separation (LLPS) is a process by which biomacromolecules,
particularly proteins, condense into a dense phase that resembles liquid droplets …

Despite the generally accepted role of the hydrophobic effect as the driving force for folding,
many intrinsically disordered proteins (IDPs), including those with hydrophobic content …

The aggregation of fusion in sarcoma (FUS) in the cytoplasm and nucleus is a pathological
feature of Amyotrophic lateral sclerosis (ALS) and Frontotemporal Dementia (FTD). Genetic …

Aqueous ionic solutions are pivotal in various scientific domains due to their natural
prevalence and vital roles in biological and chemical processes. Molecular dynamics has …