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

松尾 龍人; 荒田 敏昭*; 小田 俊郎*; 中島 健次; 河村 聖子; 菊地 龍弥; 藤原 悟

Biochemistry and Biophysics Reports (Internet), 6, p.220 - 225, 2016/07

https://doi.org/10.1016/j.bbrep.2016.04.013

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.