We attributed the faster diffusion of vitamin E in irradiated UHMWPE in SC-CO2 to the dissolution of vitamin E in the supercritical fluid and a rate of diffusion that was closer to

that of the supercritical fluid in the polymer. (C) 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2012″
“The role of interfaces and higher bands on the electronic structure of embedded semiconductor quantum dots (QDs) was investigated. The term in the multiband k.p Hamiltonian that captures the effect of interface band mixing was derived starting from the microscopic theory. It was shown, analytically and numerically, that, with such a term included, the right symmetry of the QD system can be Z-VAD-FMK molecular weight captured. It leads to splitting of otherwise degenerate energy levels of the order of several meV. The inclusion of additional higher bands beyond the ones from the standard eight-band model also leads to the reduction of symmetry from an artificially high one to the true atomistic symmetry of the system, however their quantitative effect is weaker. These results prove that the multiband k.p Hamiltonians are fully capable of describing the correct symmetry of a QD. (C) 2011 American Institute

of Physics. [doi: 10.1063/1.3631048]“
“The Sec1/munc18 protein GSK923295 family is essential for vesicle fusion in eukaryotic cells via binding to SNARE proteins. Protein kinase C modulates these interactions by phosphorylating munc18a thereby reducing its affinity to one of the central SNARE members, syntaxin-1a. The established

hypothesis is that the reduced affinity of the phosphorylated munc18a to syntaxin-1a is a result of local electrostatic repulsion between the two proteins, which interferes with their compatibility. The current study challenges this paradigm and offers a novel mechanistic explanation by revealing a syntaxin-non-binding conformation of munc18a that is induced by the phosphomimetic mutations. In the present study, using molecular Vorinostat datasheet dynamics simulations, we explored the dynamics of the wild-type munc18a versus phosphomimetic mutant munc18a. We focused on the structural changes that occur in the cavity between domains 3a and 1, which serves as the main syntaxin-binding site. The results of the simulations suggest that the free wild-type munc18a exhibits a dynamic equilibrium between several conformations differing in the size of its cavity (the main syntaxin-binding site). The flexibility of the cavity’s size might facilitate the binding or unbinding of syntaxin. In silico insertion of phosphomimetic mutations into the munc18a structure induces the formation of a conformation where the syntaxin-binding area is rigid and blocked as a result of interactions between residues located on both sides of the cavity.