Hydration effect on low-frequency protein dynamics observed in simulated neutron scattering spectra.

ABSTRACT: Hydration effects on protein dynamics were investigated by comparing the frequency dependence of the calculated neutron scattering spectra between full and minimal hydration states at temperatures between 100 and 300 K. The protein boson peak is observed in the frequency range 1-4 meV at 100 K in both states. The peak frequency in the minimal hydration state shifts to lower than that in the full hydration state. Protein motions with a frequency higher than 4 meV were shown to undergo almost harmonic motion in both states at all temperatures simulated, whereas those with a frequency lower than 1 meV dominate the total fluctuations above 220 K and contribute to the origin of the glass-like transition. At 300 K, the boson peak becomes buried in the quasielastic contributions in the full hydra

SUBMITTER: Joti Y 

PROVIDER: S-EPMC2480692 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature