Logarithmic decay in single-particle relaxation of hydrated lysozyme powder.
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 alpha relaxation. This kind of slow dynamics resembles the relaxation scenario within the beta-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.
Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Marco
M
Lagi
Piero
P
Baglioni
Sow-Hsin
SH
Chen
D000596:Amino Acids / Q000737:chemistry; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011208:Powders / Q000737:chemistry
D000596:Amino Acids; D011208:Powders; D009113:Muramidase