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Hydration Affects Both Harmonic and Anharmonic Nature of Protein Dynamics

H. Nakagawa ^*, Y. Joti  , A. Kitao   and M. Kataoka ^* 

^* Neutron Biophysics Group, Neutron Biology Research Center, Quantum Beam Science Directorate, Japanese Atomic Energy Agency, Tokai, Ibaraki 319-1195, Japan; Laboratory of Molecular Design, Institute of Molecular and Cellular Biosciences, University of Tokyo, Bunkyo-Ku, Tokyo 113-0032, Japan; Core Research for Evolutional Science and Technology, Japanese Science and Technology Agency, Bunkyo-Ku, Tokyo 113-0032, Japan; and Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan

Correspondence: Address reprint requests to Mikio Kataoka, Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. Tel.: 81-743-72-6100; Fax: 81-743-72-6109; E-mail: kataoka{at}ms.naist.jp.

To understand the effect of hydration on protein dynamics, inelastic neutron-scattering experiments were performed on staphylococcal nuclease samples at differing hydration levels: dehydrated, partially hydrated, and hydrated. At cryogenic temperatures, hydration affected the collective motions with energies lower than 5 meV, whereas the high-energy localized motions were independent of hydration. The prominent change was a shift of boson peak toward higher energy by hydration, suggesting a hardening of harmonic potential at local minima on the energy landscape. The 240 K transition was observed only for the hydrated protein. Significant quasielastic scattering at 300 K was observed only for the hydrated sample, indicating that the origin of the transition is the motion activated by hydration water. The neutron-scattering profile of the partially hydrated sample was quite similar to that of the hydrated sample at 100 K and 200 K, whereas it was close to the dehydrated sample at 300 K, indicating that partial hydration is sufficient to affect the harmonic nature of protein dynamics, and that there is a threshold hydration level to activate anharmonic motions. Thus, hydration water controls both harmonic and anharmonic protein dynamics by differing means.