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Logarithmic Decay in Single-Particle Relaxation of Hydrated Lysozyme Powder

Author(s)
Lagi, Marco; Baglioni, Piero; Chen, Sow-Hsin
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Abstract
We present the self-dynamics of protein amino acids of hydrated lysozyme powder around the physiological temperature by means of molecular dynamics simulations. The self-intermediate scattering functions of the amino acid residue center of mass display a logarithmic decay over 3 decades of time, from 2 ps to 2 ns, followed by an exponential α relaxation. This kind of slow dynamics resembles the relaxation scenario within the β-relaxation time range predicted by mode coupling theory in the vicinity of higher-order singularities. These results suggest a strong analogy between the single-particle dynamics of the protein and the dynamics of colloidal, polymeric, and molecular glass-forming liquids.
Date issued
2009-09
URI
http://hdl.handle.net/1721.1/51783
Department
Massachusetts Institute of Technology. Department of Nuclear Science and Engineering
Journal
Physical Review Letters
Publisher
American Physical Society
Citation
Lagi, Marco , Piero Baglioni, and Sow-Hsin Chen. “Logarithmic Decay in Single-Particle Relaxation of Hydrated Lysozyme Powder.” Physical Review Letters 103.10 (2009): 108102. © 2009 The American Physical Society.
Version: Final published version
ISSN
0031-9007

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