Slow Protein Dynamics to be Detected in Inelastic Neutron Scattering Spectra Studied by Molecular Simulation

Abstract

The dynamic structure factors were calculated by using the results of biomolecular simulations at the room and cryogenic temperatures. Three types of simulation, normal mode analysis, molecular dynamics in vacuum, and molecular dynamics in water were applied to HEW Lysozyme. At the room temperature, the shapes of the three dynamic structure factors are in good agreement in the high frequency regions (> 60 cm−1), but considerably different in the low frequency regions (< 60 cm−1). At the cryogenic temperature, the so‐called boson peak (∼ 30 cm−1) is observed only in the results of molecular dynamics in water. The slow dynamics of protein, found in these low frequency regions, are likely to play important roles to protein function.