A continuum-microscopic method based on IRBFs and control volume scheme for viscoelastic fluid flows

A numerical computation of continuum-microscopic model for visco-elastic flows based on the Integrated Radial Basis Function (IRBF) Control Volume and the Stochastic Simulation Techniques (SST) is reported in this paper. The macroscopic flow equations are closed by a stochastic equation for the extra stress at the microscopic level. The former are discretised by a 1D-IRBF-CV method while the latter is integrated with Euler explicit or Predictor-Corrector schemes. Modelling is very efficient as it is based on Cartesian grid, while the integrated RBF approach enhances both the stability of the procedure and the accuracy of the solution. The proposed method is demonstrated with the solution of the start-up Couette flow of the Hookean and FENE dumbbell model fluids

A CrC^{r} Closing Lemma for a Class of Symplectic Diffeomorphisms

We prove a $C^r$ closing lemma for a class of partially hyperbolic symplectic diffeomorphisms. We show that for a generic $C^r$ symplectic diffeomorphism, $r =1, 2, ...,$, with two dimensional center and close to a product map, the set of all periodic points is dense

Evidence of secondary relaxations in the dielectric spectra of ionic liquids

We investigated the dynamics of a series of room temperature ionic liquids based on the same 1-butyl-3-methyl imidazolium cation and different anions by means of broadband dielectric spectroscopy covering 15 decades in frequency (10^(-6)-10^9 Hz), and in the temperature range from 400 K down to 35 K. An ionic conductivity is observed above the glass transition temperature T_{g} with a relaxation in the electric modulus representation. Below T_{g}, two relaxation processes appear, with the same features as the secondary relaxations typically observed in molecular glasses. The activation energy of the secondary processes and their dependence on the anion are different. The slower process shows the characteristics of an intrinsic Johari-Goldstein relaxation, in particular an activation energy E_{beta}=24k_{B}T_{g} is found, as observed in molecular glasses.Comment: Major revision, submitted to Phys. Rev. Let

Loss of α-Synuclein Does Not Affect Mitochondrial Bioenergetics in Rodent Neurons.

Increased α-synuclein (αsyn) and mitochondrial dysfunction play central roles in the pathogenesis of Parkinson's disease (PD), and lowering αsyn is under intensive investigation as a therapeutic strategy for PD. Increased αsyn levels disrupt mitochondria and impair respiration, while reduced αsyn protects against mitochondrial toxins, suggesting that interactions between αsyn and mitochondria influences the pathologic and physiologic functions of αsyn. However, we do not know if αsyn affects normal mitochondrial function or if lowering αsyn levels impacts bioenergetic function, especially at the nerve terminal where αsyn is enriched. To determine if αsyn is required for normal mitochondrial function in neurons, we comprehensively evaluated how lowering αsyn affects mitochondrial function. We found that αsyn knockout (KO) does not affect the respiration of cultured hippocampal neurons or cortical and dopaminergic synaptosomes, and that neither loss of αsyn nor all three (α, β and γ) syn isoforms decreased mitochondria-derived ATP levels at the synapse. Similarly, neither αsyn KO nor knockdown altered the capacity of synaptic mitochondria to meet the energy requirements of synaptic vesicle cycling or influenced the localization of mitochondria to dopamine (DA) synapses in vivo. Finally, αsyn KO did not affect overall energy metabolism in mice assessed with a Comprehensive Lab Animal Monitoring System. These studies suggest either that αsyn has little or no significant physiological effect on mitochondrial bioenergetic function, or that any such functions are fully compensated for when lost. These results implicate that αsyn levels can be reduced in neurons without impairing (or improving) mitochondrial bioenergetics or distribution

Captura incidental de tartarugas-marinhas em currais-de-pesca no litoral do Piauí, Brasil.

CBO2010

Delineation of the Native Basin in Continuum Models of Proteins

We propose two approaches for determining the native basins in off-lattice models of proteins. The first of them is based on exploring the saddle points on selected trajectories emerging from the native state. In the second approach, the basin size can be determined by monitoring random distortions in the shape of the protein around the native state. Both techniques yield the similar results. As a byproduct, a simple method to determine the folding temperature is obtained.Comment: REVTeX, 6 pages, 5 EPS figure