RESUMEN
The vibrational density of states of single-wall carbon nanotubes (SWNT) was obtained from inelastic neutron scattering data from 0 to 225 meV. The spectrum is similar to that of graphite above 40 meV, while intratube features are clearly observed at 22 and 36 meV. An unusual energy dependence below 10 meV is assigned to contributions from intertube modes in the 2D triangular lattice of SWNT bundles, and from intertube coupling to intratube excitations. Good agreement between experiment and a calculated density of states for the SWNT lattice is found over the entire energy range.
RESUMEN
Using inelastic neutron scattering, we have observed well-defined phonon-roton ( p-r) excitations in superfluid 4He in Vycor over a wide wave-vector range, 0.3=Q=2.15 A(-1). The p-r energies and lifetimes at all temperatures are the same as in bulk liquid 4He. However, the weight of the single p-r component does not scale with the superfluid fraction rho(S)(T)/rho as it does in the bulk. In particular, we observe a p-r excitation above T(c) = 1.952 K, where rho(s)(T) = 0 in Vycor. This suggests, if the p-r excitation intensity scales with the Bose condensate, that there is a separation of the Bose-Einstein condensation temperature and the superfluid transition temperature T(c) of 4He in Vycor.
RESUMEN
Quasielastic neutron scattering experiments performed on yeast phosphoglycerate kinase in the native form and denatured in 1.5 M guanidinium chloride reveal a change in the fast (picosecond time scale) diffusive internal dynamics of the protein. The momentum and energy transfer dependences of the scattering for both states are fitted by an analytical model in which, on the experimentally accessible picosecond time scale and angstrom length scale, the dynamics of a fraction of the nonexchangeable hydrogens in the protein is described as a superposition of vibrations with uniform diffusion in a sphere, the rest of the hydrogens undergoing only vibrational motion. The fraction diffusing changes, from approximately 60% in the native protein to approximately 82% in the denatured protein. The radius of the sphere also changes slightly, from approximately 1.8 A in the native protein to approximately 2.2 A in the denatured protein. Possible implications of these results for the general protein folding problem are discussed.
Asunto(s)
Fosfoglicerato Quinasa/química , Termodinámica , Guanidina , Guanidinas , Hidrógeno , Matemática , Desnaturalización Proteica , Saccharomyces cerevisiae/enzimología , Dispersión de RadiaciónRESUMEN
Incoherent quasi-elastic neutron scattering is applied to study the local diffusion and chain dynamics of L-alpha-diplamiotylphosphatidylcholine molecules in oriented model membranes. Different motions are distinguished by changing the hydration of the multilayers as well as by measuring below and above the gel-to-liquid crystalline phase transition. The time range of the utilized time-of-flight spectrometer permits to observe two types of motion to be observed more closely: chain defect motions and the local diffusion of the whole molecule in its solvation cage. Oriented lipid membranes are a useful system for the observation of chain defects, as they can be macroscopically oriented, in contrast to most polymers. As a representative model for a chain defect a kink is chosen and the corresponding scattering functions are derived. The kink motion can explain the entire dynamics seen in the gel phase, and the lifetime of such a defect was found to be 10-15 ps, in good agreement with theoretical predictions. On the other hand the dynamics in the liquid crystalline phase cannot be explained even by a superposition of several kinks and thus requires the consideration of an additional motion: the local diffusion of the molecule in its solvation cage. The size of the solvation cage is increasing with multilayer hydration and reduced temperature. Particularly interesting in view of recent discussions about the origin of the short-range repulsive forces between membranes is the experimental finding of an out-of-plane motion with an amplitude of 1-1.5 A, which cannot be explained by the undulation of the whole membrane.