BACKGROUND Biomolecular mechanisms are typically inferred from static structural
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …

Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

Material properties of phase-separated biomolecular condensates, enriched with disordered
proteins, dictate many cellular functions. Contrary to the progress made in understanding the …

Liquid–liquid phase separation of flexible biomolecules has been identified as a ubiquitous
phenomenon underlying the formation of membraneless organelles that harbor a multitude …

Proteins that undergo liquid–liquid phase separation (LLPS) have been shown to play a
critical role in many physiological functions through formation of condensed liquid-like …

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

Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of
disparate client proteins. This implicates Hsp90 in diverse biological processes that require …

One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

Proteins and synthetic polymers can undergo phase transitions in response to changes to
intensive solution parameters such as temperature, proton chemical potentials (pH), and …

The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …