Logarithmic Decay in Single-Particle Relaxation of Hydrated Lysozyme Powder
Author(s)Lagi, Marco; Baglioni, Piero; Chen, Sow-Hsin
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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.
DepartmentMassachusetts Institute of Technology. Department of Nuclear Science and Engineering
Physical Review Letters
American Physical Society
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.
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