Protein flexibility, which is required for biological function, is strongly mediated by its natural solvent � water. In spite of ongoing progress in this field, a clear mechanistic picture describing how water/solvent motions affect a protein has not yet emerged. However, long range correlated vibrational motions in the hydrogen bond network of water, identified in a recent first principles simulation of the pure liquid, might play a significant role for the coupling between water and solvated proteins. Specifically, such a coupling is held responsible for experimentally observed changes in the terahertz absorption of the solvation water of proteins. Here, we will try to complete this picture by characterizing the hydrogen bond network vibrations of water in the presence of a protein and by quantifying the degree of correlated motion between water molecules and the solvated protein.

Correlated intermolecular motion in solvation water of biomolecules

243rd National Meeting (2012)

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