Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

In stark contrast to foldable proteins with a unique folded state, intrinsically disordered
proteins and regions (IDPs) persist in perpetually disordered ensembles. Yet an IDP …

The abundance of intrinsic disorder in the protein realm and its role in a variety of
physiological and pathological cellular events have strengthened the interest of the scientific …

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 …

While in the vast majority of cases fluorescence in biological matter has been attributed to
aromatic or conjugated groups, peptides associated with neurodegenerative diseases, such …

Intrinsically disordered proteins (IDPs) that lie close to the empirical boundary separating
IDPs and folded proteins in Uversky's charge–hydropathy plot may behave as “marginal …

The physical chemistry of liquid-liquid phase separation (LLPS) of polymer solutions bears
directly on the assembly of biologically functional dropletlike bodies from proteins and …

High internal phase emulsions (HIPEs) have recently been investigated for applications in
food areas: plant proteins, polysaccharides, and commercial surfactants have been used as …

Intrinsic protein fluorescence is inextricably linked to the near-UV autofluorescence of
aromatic amino acids. Here we show that a novel deep-blue autofluorescence (dbAF) …

We present an analytical theory to compute conformations of heteropolymers—applicable to
describe disordered proteins—as a function of temperature and charge sequence. The …