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Updated: Aug 16, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Onsets of anharmonicity in protein dynamics
J H Roh1, V N Novikov, R B Gregory
1Department of Polymer Science, The University of Akron, Akron, OH 44325-3909, USA.
Abstract:
Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at T approximately 100 K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at T approximately 200-230 K, is only observed at a hydration level h greater than approximately 0.2 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.
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