Effect of hydration on protein dynamics studied by neutron inelastic scattering

Nakagawa, Hiroshi   

Proteins, molecular machines that contribute to almost all living phenomena, primarily function in an aqueous milieu at ambient temperatures. It has been reported that proteins cannot function at cryogenic temperature cryogenic temperatures or at low hydration levels, which strongly implies that both thermal fluctuations and hydration affect protein function. In order to understand the molecular mechanisms that underlie cellular biology, it is essential to examine protein dynamics in aqueous environments. Inelastic neutron scattering (INS) allows protein dynamics to be examined at pico- to nanosecond timescales.