  We present the self-dynamics of protein amino acids of hydrated lysozyme
powder around the physiological temperature by means of molecular dynamics (MD)
simulations. The self-intermediate scattering functions (SISF) of the amino
acid residue center-of-mass and of the protein hydrogen atoms display a
logarithmic decay over 3 decades of time, from 2 picoseconds to 2 nanoseconds,
followed by an exponential alpha-relaxation. This kind of slow dynamics
resembles the relaxation scenario within the beta-relaxation time range
predicted by the mode coupling theory (MCT) 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.
