Intrinsically disordered proteins (IDPs) differ from “normal” ordered proteins at several levels,
structural, functional and conformational. Amino acid biases characteristic for IDPs …

Intrinsically disordered proteins (IDPs) defy the structure–function paradigm as they fulfill
essential biological functions while lacking well‐defined secondary and tertiary structures …

Trimethylamine n-oxide (TMAO) is a naturally occurring osmolyte that stabilizes proteins and
offsets the destabilizing effects of urea. To investigate the molecular mechanism of these …

Proteins are very sensitive to their solvent environments. Urea is a common chemical
denaturant of proteins, yet some animals contain high concentrations of urea. These animals …

Nature has selected osmolytes to protect intracellular macromolecules exposed to
denaturing conditions and stabilize proteins. Osmolytes are small naturally occurring …

The glucocorticoid receptor (GR) belongs to the superfamily of ligand-activated transcription
factors, the nuclear hormone receptors. Like other members of the family, the GR possesses …

This paper overviews solution additives that affect protein stability and aggregation during
refolding, heating, and freezing processes. Solution additives are mainly grouped into two …

The N-terminal domains (NTDs) of many members of the nuclear hormone receptor (NHR)
family contain potent transcription-activating functions (AFs). Knowledge of the mechanisms …

Cell cytoplasm contains high concentrations of high-molecular-weight components that
occupy a substantial part of the volume of the medium (crowding conditions). The effect of …

Organisms use organic molecules called osmolytes to adapt to environmental conditions. In
vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are …