Abstract
Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at , is only observed at a hydration level greater than and is ascribed to the activation of an additional relaxation process. Its variation with hydration correlates well with variations of catalytic activity suggesting that the relaxation process is directly related to the activation of modes required for protein function.
- Received 5 August 2004
DOI:https://doi.org/10.1103/PhysRevLett.95.038101
©2005 American Physical Society