The low-temperature dynamic crossover phenomenon in protein hydration water: simulations vs experiments

Article Abstract:

Molecular dynamics have shown that the low-temperature crossover phenomenon is because of the average translational motion of all the water molecules in the hydration layer, not due to the long-range proton diffusion coupled to the motion of the Bjerrum-type defects. Neutron scattering and NMR have quantitatively accounted for the temperature dependence of the experimental data from a realistic powder model.

Analysis, Water, Molecular dynamics, Hydrogen bonding, Hydrogen bonds, Lysozyme, Mechanical properties, Structure, Chemical properties, Hydration (Chemistry)

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Amphiphilic self-assemblies decorated by nucleobases

Article Abstract:

The aggregation behavior of different 1-R,2-R-sn-glycero-3-phosphatidyl-nucleosides, where R = 8 (Di[C.sub.8]PN) or R = DLPN and N is either adenosine or uridine, a complementary pair in RNA) is compared. The nucleic functionalization has provided an additional parameter to control self-assembly through specific interactions among the polar heads and have altered the aggregation thresholds.

Biological Product (except Diagnostic) Manufacturing, Nucleic Acid Derivatives, Usage, Transmission electron microscopes, Phospholipases, Nucleosides, Crystallization, Surface tension

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