Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …

The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Dynamic ensembles of macromolecules mediate essential processes in biology.
Understanding the mechanisms driving the function and molecular interactions …

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 …

Dipolar EPR spectroscopy (DEER and other techniques) enables the structural
characterization of macromolecular and biological systems by measurement of distance …

Solvent accessible surface area (SASA) of proteins has always been considered as a
decisive factor in protein folding and stability studies. It is defined as the surface …

The dimensions of unfolded and intrinsically disordered proteins are highly dependent on
their amino acid composition and solution conditions, especially salt and denaturant …

Liquid-liquid phase separation (LLPS) of proteins is thought to be a primary driving force for
the formation of membraneless organelles, which control a wide range of biological …

Spectroscopic studies have identified a number of proteins that appear to retain significant
residual structure under even strongly denaturing conditions. Intrinsic viscosity …

The microtubule-associated protein tau stabilizes microtubules in its physiological role,
whereas it forms insoluble aggregates (paired helical filaments) in Alzheimer's disease …