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Report No.
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Effect of hydration on protein dynamics

Kataoka, Mikio; Nakagawa, Hiroshi  

Proteins are biologically functional elements in the living organisms. Most proteins work in an aqueous environment. Here, we will review the effect of hydration on protein dynamics. We could classify the wide neutron spectrum into the hydration uncoupled and coupled modes. The former is comprised of localized motions, such as methyl rotation and CH bending, which corresponds to vibrational spectrum observed by IR region. The latter contains the collective motions spread over whole protein observed in the low energy spectral region. Significant increase of atomic mean-square displacement at around 240 K, which is dynamical transition, was induced by hydration. Hydration hardens the harmonic properties of protein while softens protein by acquisition of anharmonic motions. At the ambient temperature, hydration affects the surface shell of the protein structure, indicating the importance of the interaction between the protein surface and hydration water for the protein dynamics. The dynamical coupling of protein with hydration water contributes to the biologically functional mobility of protein.

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