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Special Issue on Advanced neutron scattering and complementary techniques to study biological systems. Contributions from the meetings, "Neutrons in Biology", STFC Rutherford Appleton Laboratory, Didcot, UK, 11-13 July and "Proteins At Work 2007", Perugia, Italy, 28-30 May 2007
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Probing the Thermal Stability of Lysozyme in Crowded Environments: Tracking Lindemann Criterion
No full textProbing the Thermal Stability of Lysozyme in Crowded Environments: Tracking Lindemann Criterio
Thermal fluctuations of DNA enclosed by glycerol-water glassy matrices: an elastic neutron scattering investigation
No full textLow-frequency Vibrational Anomalies in Beta-lactoglobulin: Contribution of Different Hydrogen Classes Revealed by Inelastic Neutron Scattering
No full textInfluence of the “Host-guest” interactions on the mobility of Genistein/Beta Cyclodextrin inclusion complex
No full textDynamics of Different Hydrogen Classes in Beta-lactoglobulin: A Quasielastic Neutron Scattering Investigation
No full textElastic neutron scattering study of proton dynamics in glycerol
No full textA recent neutron scattering investigation on lysozyme embedded in glycerol-water mixtures has shown that solvent dynamics is crucial in determining the dynamical properties of the biomolecule itself (Biophys. J. 83 (2002) 1157). To better understand the role played by solvent, we have performed an elastic incoherent neutron scattering (INS) experiment as a function of the temperature on pure glycerol. To directly compare the dynamics of the solvated protein and that of the pure solvent, we settled the same experimental conditions and applied the same data analysis procedure as in Paciaroni et al. (Biophys. J. 83 (2002) 1157). By using a double-well model and taking into account for the global molecular diffusion, we exploited the measured intensity to estimate the mean square displacements (MSD) of glycerol hydrogen atoms. We found that the total MSD deviate from the low-temperature vibrational harmonic trend at approximately T = 235 K, consistent with the value of the critical temperature reported in literature (Phys. Rev. E 55 (1997) 3183). The present investigation suggests that the internal dynamics of glycerol molecules, i.e. the vibrations and reorientations of hydrogen atoms relative to the molecular centre of mass (c.o.m.), can be put in relationship with the protein dynamics
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