AI Article Synopsis
- The dynamics of hydrated proteins are crucial for biological activity, as they correspond with changes in hydrogen bonds and amino acid motions.
- The study reveals a strong connection between protein motion and the surrounding hydration water, showing that the water's dynamics are influenced by the protein's collective movements.
- This research provides clear evidence of a robust interaction between proteins and hydration water, highlighting a previously suggested dynamical coupling that has significant implications for understanding protein function.
Article Abstract
Picosecond time scale dynamics of hydrated proteins has been connected with the onset of biological activity as it coincides with solvent-solute hydrogen bond rearrangements and amino acid rotational relaxation time scales. The presence and fluctuations of protein hydration water (PHW) largely influence protein motions that are believed to be slaved to those of the solvent, yet to date, how protein and hydration water dynamics are coupled remains unclear. Here, we provide a significant advance in characterizing this coupling; we present the first full study of both the longitudinal and transverse coherent collective motions in a protein-solvent system. The data show unexpectedly the presence in the water dynamics of collective modes belonging to the protein. The properties of these modes, in particular, their propagation velocities and amplitudes, indicate a strengthening of the interactions and a higher rigidity of the network of solvent molecules close to the protein surface. Accordingly, the present study presents the most compelling and clear evidence of a very strong dynamical coupling between a protein and its hydration water, previously suggested by studies using various experimental techniques.
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| http://dx.doi.org/10.1021/jz500023e | DOI Listing |
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