Berlin 2024 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 4: Computational Biophysics I
BP 4.4: Vortrag
Montag, 18. März 2024, 15:45–16:00, H 0112
Validating the Protein Hydration Shell against Small-angle Scattering Data - Effects of Water Models, Force Fields, and Surface Composition — •Johanna-Barbara Linse and Jochen S. Hub — Theoretical Physics and Center for Biophysics, Saarland University, Saarbrücken, 66123, Germany
The proteins hydration shell plays key roles in protein stability and function. So far, it remained unclear whether hydration shells predicted by explicit-solvent molecular dynamics (MD) simulations match experimental conditions, as precise experimental data on hydration shell structures were limited. Small-angle scattering (SAS) experiments provide insight into hydration shell properties, because the detected radius of gyration (Rg) and zero-angle scattering (I0) depend on the contrast between the hydration shell and the solvent. Using explicit-solvent MD simulations and SAS calculations, we calculated Rg values for five proteins, evaluating 18 combinations of protein force fields and water models. Validation of the results against consensus data from a round-robin benchmark project revealed remarkable agreement between MD simulations and experiments, depending on the choice of force field and water model. Furthermore, we investigated the influence of amino acid surface composition of proteins on the hydration shell contrast, providing contrast scores for 20 amino acids. Our studies show that explicit-solvent SAS calculations and consensus SAS data provide a novel routes for scrutinizing the proteins hydration shell and for predicting the amino acid effects on the hydration shell structure.