Onsets of anharmonicity in protein dynamics

J. H. Roh; V. N. Novikov; R. B. Gregory; J. E. Curtis; Z. Chowdhuri; A. P. Sokolov

doi:10.1103/PhysRevLett.95.038101

Onsets of anharmonicity in protein dynamics

J. H. Roh, V. N. Novikov, R. B. Gregory, J. E. Curtis, Z. Chowdhuri, A. P. Sokolov

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227 Scopus citations

Abstract

Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at Tâ 100K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at Tâ 200â€"230K, is only observed at a hydration level h greater than â 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.

Original language	English
Article number	038101
Journal	Physical Review Letters
Volume	95
Issue number	3
DOIs	https://doi.org/10.1103/PhysRevLett.95.038101
State	Published - Jul 15 2005
Externally published	Yes

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AU - Roh, J. H.

AU - Novikov, V. N.

AU - Gregory, R. B.

AU - Curtis, J. E.

AU - Chowdhuri, Z.

AU - Sokolov, A. P.

PY - 2005/7/15

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AB - Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at Tâ 100K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at Tâ 200â€"230K, is only observed at a hydration level h greater than â 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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Onsets of anharmonicity in protein dynamics

Abstract

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