How protein hydration depends on amino acid composition, peptide conformation, and force fields.

ABSTRACT: The protein hydration shell is a key mediator of processes such as molecular recognition, protein folding, and proton transfer. How solvent-exposed amino acids shape the hydration shell structure is not well understood. We combine molecular dynamics simulations with explicit-solvent predictions of small-angle x-ray scattering (SAXS) curves to quantify the contributions of all 20 proteinogenic amino acids to the hydration shell of the globular GB3 domain and the intrinsically disordered protein (IDP) XAO. We focus on two quantities encoded by SAXS curves: the hydration shell effect on the radius of gyration and the electron density contrast between protein and solvent. We derive an amino acid-specific contrast score, revealing that acidic residues generate the strongest contrast with 1-1.5

SUBMITTER: Linse JB 

PROVIDER: S-EPMC12821034 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature