Viruses infect all kingdoms of life; their genomes vary from DNA to RNA and in size from 2kB
to 1 MB or more. Viruses frequently employ disordered proteins, that is, protein products of …

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are
abundant in all species. They play critical roles in many cellular processes, including …

It is now increasingly evident that a large fraction of the human proteome comprises proteins
that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have …

Intrinsically disordered proteins (IDPs) can display a broad spectrum of binding modes and
highly variable binding affinities when interacting with both biological and nonbiological …

Atomistic-level understanding of surface hydration mediating protein–protein interactions
and ligand binding has been a challenge due to the dynamic nature of water molecules near …

The net electrostatic charge (Z) of a folded protein in solution represents a bird's eye view of
its surface potentials—including contributions from tightly bound metal, solvent, buffer, and …

The 1918 influenza A virus (IAV) caused the worst flu pandemic in human history. Non-
structural protein 1 (NS1) is an important virulence factor of the 1918 IAV and antagonizes …

The circadian clock times cellular processes to the day/night cycle via a Transcription-
Translation negative Feedback Loop (TTFL). However, a mechanistic understanding of the …

The human zinc‐and iron‐regulated transport protein 4 (hZIP4) protein is the major plasma
membrane protein responsible for the uptake of zinc in the body, and as such it plays a key …

Protein-protein interactions are involved in a wide range of cellular processes. These
interactions often involve intrinsically disordered proteins (IDPs) and protein binding …