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Difference in the hydration water mobility around F-actin and myosin subfragment-1 studied by quasielastic neutron scattering

Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Nakajima, Kenji  ; Kawamura, Seiko; Kikuchi, Tatsuya; Fujiwara, Satoru

Hydration water is essential for a protein to perform its biological function properly. In this study, the dynamics of hydration water around F-actin and myosin subfragment-1 (S1), which are the partner proteins playing a major role in various cellular functions related to cell motility, was characterized by incoherent quasielastic neutron scattering (QENS). The QENS spectra of hydration water around F-actin and S1 provided the translational diffusion coefficient, the residence time, and the rotational correlation time. The differences in these parameters indicate a significant difference in mobility of the hydration water between S1 and F-actin: S1 has the typical hydration water, the mobility of which is reduced compared with that of bulk water, while F-actin has the unique hydration water, the mobility of which is close to that of bulk water rather than the typical hydration water around proteins.

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