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Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

ABSTRACT: We present a detailed analysis of the picosecond-to-nanosecond motions of green fluorescent protein (GFP) and its hydration water using neutron scattering spectroscopy and hydrogen/deuterium contrast. The analysis reveals that hydration water suppresses protein motions at lower temperatures (<~ 200 K), and facilitates protein dynamics at high temperatures. Experimental data demonstrate that the hydration water is harmonic at temperatures <~ 180-190 K and is not affected by the proteins' methyl group rotations. The dynamics of the hydration water exhibits changes at ~ 180-190 K that we ascribe to the glass transition in the hydrated protein. Our results confirm significant differences in the dynamics of protein and its hydration water at high temperatures: on the picosecond-to-nanosecond timescale, the hydration water exhibits diffusive dynamics, while the protein motions are localized to <~3 Å. The diffusion of the GFP hydration water is similar to the behavior of hydration water previously observed for other proteins. Comparison with other globular proteins (e.g., lysozyme) reveals that on the timescale of 1 ns and at equivalent hydration level, GFP dynamics (mean-square displacements and quasielastic intensity) are of much smaller amplitude. Moreover, the suppression of the protein dynamics by the hydration water at low temperatures appears to be stronger in GFP than in other globular proteins. We ascribe this observation to the barrellike structure of GFP.

SUBMITTER: Nickels JD

PROVIDER: S-EPMC3471459 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

Nickels Jonathan D JD O'Neill Hugh H Hong Liang L Tyagi Madhusudan M Ehlers Georg G Weiss Kevin L KL Zhang Qiu Q Yi Zheng Z Mamontov Eugene E Smith Jeremy C JC Sokolov Alexei P AP

Biophysical journal 20121002 7

We present a detailed analysis of the picosecond-to-nanosecond motions of green fluorescent protein (GFP) and its hydration water using neutron scattering spectroscopy and hydrogen/deuterium contrast. The analysis reveals that hydration water suppresses protein motions at lower temperatures (<~ 200 K), and facilitates protein dynamics at high temperatures. Experimental data demonstrate that the hydration water is harmonic at temperatures <~ 180-190 K and is not affected by the proteins' methyl g ...[more]

PMID: 23062349

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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.

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Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

Publications

Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

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