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

ABSTRACT: 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 including muscle contraction, was characterized by incoherent quasielastic neutron scattering (QENS). The QENS measurements on the D₂O- and H₂O-solution samples of F-actin and S1 provided the spectra of hydration water, from which the translational diffusion coefficient (D_T), the residence time (?_T), and the rotational correlation time (?_R) were evaluated. The D_T value of the hydration water of S1 was found to be much smaller than that of the hydration water of F-actin while the ?_T values were similar between S1 and F-actin. On the other hand, the ?_R values of the hydration water of S1 was found to be larger than that of the hydration water of F-actin. It was also found that the D_T and ?_R values of the hydration water of F-actin are similar to those of bulk water. These results suggest 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.

SUBMITTER: Matsuo T

PROVIDER: S-EPMC5600338 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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

Matsuo Tatsuhito T Arata Toshiaki T Oda Toshiro T Nakajima Kenji K Ohira-Kawamura Seiko S Kikuchi Tatsuya T Fujiwara Satoru S

Biochemistry and biophysics reports 20160430

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 including muscle contraction, was characterized by incoherent quasielastic neutron scattering (QENS). The QENS measurements on the D<sub>2</sub>O- and H<sub>2</sub>O-solution samples of F-actin and S1 provided th ...[more]

PMID: 28955880

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Project description:Water dynamics in inorganic nanotubes is studied by neutron scattering technique. Two types of aluminosilicate nanotubes are investigated: one is completely hydrophilic on the external and internal surfaces (IMO-OH) while the second possesses an internal cavity which is hydrophobic due to the replacement of Si-OH bonds by Si-CH3 ones (IMO-CH3), the external surface being still hydrophilic. The samples have internal radii equal to 7.5 and 9.8 Å, respectively. By working under well-defined relative humidity (RH) values, water dynamics in IMO-OH was revealed by quasi-elastic spectra as a function of the filling of the interior of the tubes. When one water monolayer is present on the inner surface of the tube, water molecules can jump between neighboring Si-OH sites on the circumference by 2.7 Å. A self-diffusion is then measured with a value (D = 1.4 × 10-5 cm2 s-1) around half of that in bulk water. When water molecules start filling also the interior of the tubes, a strong confinement effect is observed, with a confinement diameter (6 Å) of the same order of magnitude as the radius of the nanotube (7.5 Å). When IMO-OH is filled with water, the H-bond network is very rigid, and water molecules are immobile on the timescale of the experiment. For IMO-OH and IMO-CH3, motions of the hydroxyl groups are also evidenced. The associated relaxation time is of the order of 0.5 ps and is due to hindered rotations of these groups. In the case of IMO-CH3, quasi-elastic spectra and elastic scans are dominated by the motions of methyl groups, making the effect of the water content on the evolution of the signals negligible. It was however possible to describe torsions of methyl groups, with a corresponding rotational relaxation time of 2.6 ps. The understanding of the peculiar behavior of water inside inorganic nanotubes has implications in research areas such as nanoreactors. In particular, the locking of motions inside IMO-OH when it is filled with water prevents its use under these conditions as a nanoreactor, while the interior of the IMO-CH3 cavity is certainly a favorable place for confined chemical reactions to take place.

Dataset Information

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

Publications

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

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