Efficient Algorithms for Universal Quantum Simulation

A universal quantum simulator would enable efficient simulation of quantum dynamics by implementing quantum-simulation algorithms on a quantum computer. Specifically the quantum simulator would efficiently generate qubit-string states that closely approximate physical states obtained from a broad class of dynamical evolutions. I provide an overview of theoretical research into universal quantum simulators and the strategies for minimizing computational space and time costs. Applications to simulating many-body quantum simulation and solving linear equations are discussed

"Dark energy" in the Local Void

The unexpected discovery of the accelerated cosmic expansion in 1998 has filled the Universe with the embarrassing presence of an unidentified "dark energy", or cosmological constant, devoid of any physical meaning. While this standard cosmology seems to work well at the global level, improved knowledge of the kinematics and other properties of our extragalactic neighborhood indicates the need for a better theory. We investigate whether the recently suggested repulsive-gravity scenario can account for some of the features that are unexplained by the standard model. Through simple dynamical considerations, we find that the Local Void could host an amount of antimatter ($\sim5\times10^{15}\,M_\odot$) roughly equivalent to the mass of a typical supercluster, thus restoring the matter-antimatter symmetry. The antigravity field produced by this "dark repulsor" can explain the anomalous motion of the Local Sheet away from the Local Void, as well as several other properties of nearby galaxies that seem to require void evacuation and structure formation much faster than expected from the standard model. At the global cosmological level, gravitational repulsion from antimatter hidden in voids can provide more than enough potential energy to drive both the cosmic expansion and its acceleration, with no need for an initial "explosion" and dark energy. Moreover, the discrete distribution of these dark repulsors, in contrast to the uniformly permeating dark energy, can also explain dark flows and other recently observed excessive inhomogeneities and anisotropies of the Universe.Comment: 6 pages, accepted as a Letter to the Editor by Astrophysics and Space Scienc

Differences on the inhibitory specificities of H-Ras, K-Ras, and N-Ras (N17) dominant negative mutants are related to their membrane microlocalization.

Ras GTPases include the isoforms H-Ras, K-Ras, and N-Ras. Despite their great biochemical and biological similarities, evidence is mounting suggesting that Ras proteins may not be functionally redundant. A widespread strategy for studying small GTPases is the utilization of dominant inhibitory mutants that specifically block the activation of their respective wild-type proteins. As such, H-Ras N17 has proved to be extremely valuable as a tool to probe Ras functions. However, a comparative study on the inhibitory specificities of H-, K-, and N-Ras N17 mutants has not been approached thus far. Herein, we demonstrate that H-, K-, and N-Ras N17 mutants exhibit markedly distinct inhibitory effects toward H-, K-, and N-Ras. H-Ras N17 can effectively inhibit the activation of all three isoforms. K-Ras N17 completely blocks the activation of K-Ras and is only slightly inhibitory on H-Ras. N-Ras N17 can mainly inhibit N-Ras activation. In light of the recent data on the compartmentalization of H-Ras and K-Ras in the plasma membrane, here we present for the first time a description of N-Ras cellular microlocalization. Overall, our results on Ras N17 mutants specificities exhibit a marked correlation with the localization of the Ras isoforms to distinct membrane microdomains

The Rho family GTPase Cdc42 regulates the activation of Ras/MAP kinase by the exchange factor Ras-GRF.

The Ras guanine-nucleotide exchange factor Ras-GRF/Cdc25(Mn) harbors a complex array of structural motifs that include a Dbl-homology (DH) domain, usually found in proteins that interact functionally with the Rho family GTPases, and the role of which is not yet fully understood. Here, we present evidence that Ras-GRF requires its DH domain to translocate to the membrane, to stimulate exchange on Ras, and to activate mitogen-activated protein kinase (MAPK). In an unprecedented fashion, we have found that these processes are regulated by the Rho family GTPase Cdc42. We show that GDP- but not GTP-bound Cdc42 prevents Ras-GRF recruitment to the membrane and activation of Ras/MAPK, although no direct association of Ras-GRF with Cdc42 was detected. We also demonstrate that catalyzing GDP/GTP exchange on Cdc42 facilitates Ras-GRF-induced MAPK activation. Moreover, we show that the potentiating effect of ionomycin on Ras-GRF-mediated MAPK stimulation is also regulated by Cdc42. These results provide the first evidence for the involvement of a Rho family G protein in the control of the activity of a Ras exchange factor