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.