SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell.

ABSTRACT: Water molecules in the immediate vicinity of biomacromolecules, including proteins, constitute a hydration layer characterized by physicochemical properties different from those of bulk water and play a vital role in the activity and stability of these structures, as well as in intermolecular interactions. Previous studies using solution scattering, crystallography, and molecular dynamics simulations have provided valuable information about the properties of these hydration shells, including modifications in density and ionic concentration. Small-angle scattering of x-rays (SAXS) and neutrons (SANS) are particularly useful and complementary techniques to study biomacromolecular hydration shells due to their sensitivity to electronic and nuclear scattering-length density fluctuations, respe

SUBMITTER: Kim HS 

PROVIDER: S-EPMC4880798 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature