Self-assembled peptide nanostructures have been increasingly exploited as functional
materials for applications in biomedicine and energy. The emergent properties of these …

Highlights•Improvements in all-atom simulations and implicit solvent models now allow IDP
simulations with realistic dimensions to be performed.•Native-centric coarse-grained …

The formation of membraneless organelles in cells commonly occurs via liquid–liquid phase
separation (LLPS) and is in many cases driven by multivalent interactions between …

The sustenance of life depends on the high degree of organization that prevails through
different levels of living organisms, from subcellular structures such as biomolecular …

The dynamics of proteins, which are essential for both folding and function, are known to be
strongly dependent on solvent viscosity or friction. However, an increasing number of …

Single-molecule Förster resonance energy transfer (FRET) is a versatile technique for
probing the structure and dynamics of biomolecules even in heterogeneous ensembles …

Förster resonance energy transfer (FRET) is a powerful tool for elucidating both structural
and dynamic properties of unfolded or disordered biomolecules, especially in single …

Thermodynamic and kinetic properties are of critical importance for the applicability of
computational models to biomolecules such as proteins. Here we present an extensive …

Experimental studies on intrinsically disordered and unfolded proteins have shown that in
isolation they typically have low populations of secondary structure and exhibit distance …

Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently
emerged as major therapeutic targets for various diseases. Unlike traditional proteins that …