Onsets of Anharmonicity in Protein Dynamics

J. H. Roh, V. N. Novikov, R. B. Gregory, J. E. Curtis, Z. Chowdhuri, and A. P. Sokolov
Phys. Rev. Lett. 95, 038101 – Published 12 July 2005

Abstract

Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at T100K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at T200230K, is only observed at a hydration level h greater than 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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  • Received 5 August 2004

DOI:https://doi.org/10.1103/PhysRevLett.95.038101

©2005 American Physical Society

Authors & Affiliations

J. H. Roh1, V. N. Novikov1,4, R. B. Gregory2, J. E. Curtis3, Z. Chowdhuri3, and A. P. Sokolov1,*

  • 1Department of Polymer Science, The University of Akron, Akron, Ohio 44325-3909, USA
  • 2Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
  • 3National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA
  • 4IA&E, Russian Academy of Sciences, Novosibirsk, 630090, Russia

  • *Corresponding author.

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Vol. 95, Iss. 3 — 15 July 2005

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