Measurement of the η\eta -η′\eta' mixing angle in π−\pi^{-} and K−K^{-} beams with GAMS-4π4\pi Setup

The results of mixing angle measurement for $\eta'$, $\eta$ mesons generated in charge exchange reactions with $\pi^{-}$ and $K^{-}$ beams are preseneted. When the $\eta'$, $\eta$ mesons are described in nonstrange(NS)--strange(S) quark basis the $\pi^{-}$ and $K^{-}$ beams allow to study $|\eta_{q}>$ and $|\eta_{s}>$ parts of the meson wave function. The cross section ratio at $t'=0$ (GeV/c)$^{2}$ in the $\pi^{-}$ beam is $R_{\pi}(\eta'/\eta)= 0.56 \pm 0.04$, results in mixing angle $\phi_{P} = (36.8 \pm 1.)^{o}$. For $K^{-}$ beam the ratio is $R_{K}(\eta'/\eta)= 1.30 \pm 0.16$. It was found that gluonium content in $\eta'$ is $\sin^{2}\psi_{G}= 0.15 \pm 0.06$. The experiment was carried out with GAMS-4$\pi$ Setup.Comment: 6 pages, 4 figures, 1 table, to be submitted in European physical journal C. Minor changes, the Bibliography extende

Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function

Background Human S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins that are associated with many diseases including cancer, chronic inflammation and neurological disorders. S100A12 is an important factor in host/parasite defenses and in the inflammatory response. Like several other S100 proteins, it binds zinc and copper in addition to calcium. Mechanisms of zinc regulation have been proposed for a number of S100 proteins e.g. S100B, S100A2, S100A7, S100A8/9. The interaction of S100 proteins with their targets is strongly dependent on cellular microenvironment. Results The aim of the study was to explore the factors that influence S100A12 oligomerization and target interaction. A comprehensive series of biochemical and biophysical experiments indicated that changes in the concentration of calcium and zinc led to changes in the oligomeric state of S100A12. Surface plasmon resonance confirmed that the presence of both calcium and zinc is essential for the interaction of S100A12 with one of its extracellular targets, RAGE – the Receptor for Advanced Glycation End products. By using a single-molecule approach we have shown that the presence of zinc in tissue culture medium favors both the oligomerization of exogenous S100A12 protein and its interaction with targets on the cell surface. Conclusion We have shown that oligomerization and target recognition by S100A12 is regulated by both zinc and calcium. Our present work highlighted the potential role of calcium-binding S100 proteins in zinc metabolism and, in particular, the role of S100A12 in the cross talk between zinc and calcium in cell signaling

Insight into resolution enhancement in generalized two-dimensional correlation spectroscopy

Generalized two-dimensional correlation spectroscopy (2D-COS) can be used to enhance spectral resolution in order to help differentiate highly overlapped spectral bands. Despite the numerous extensive 2D-COS investigations, the origin of the 2D spectral resolution enhancement mechanism(s) is not completely understood. In the work here, we studied the 2D-COS of simulated spectra in order to develop new insights into the dependence of 2D-COS spectral features on the overlapping band separations, their intensities and bandwidths, and their band intensity change rates. We found that the features in the 2D-COS maps that are derived from overlapping bands were determined by the spectral normalized half-intensities and the total intensity changes of the correlated bands. We identified the conditions required to resolve overlapping bands. In particular, 2D-COS peak resolution requires that the normalized half-intensities of a correlating band have amplitudes between the maxima and minima of the normalized half-intensities of the overlapping bands. © 2013 Society for Applied Spectroscopy

Semiclassical model of ultrafast photoisomerization reactions

In this letter we propose a model which explains ultrafast and efficient photoisomerization reactions as driven by transitions between quasistationary states of one dimensional (1D) double well potential of an excited electronic state. This adiabatic potential is formed as a result of doubly crossing of a decay diabatic potential of the ground electronic state and a bound diabatic potential of the excited state. We calculate the eigenstates and eigenfunctions using the semiclassical connection matrices at the turning and crossing points and the shift matrices between these points. The transitions between the localized in the wells below the adiabatic barrier states are realized by the tunneling and by the double non-adiabatic transitions via the crossing points processes. Surprisingly the behavior with the maximum transition rate keeps going even for the states relatively far above the barrier (2 -4 times the barrier height). Even though a specific toy model is investigated here, when properly interpreted it yields quite reasonable values for a variety of measured quantities, such as a reaction quantum yield, and conversion time.Comment: 9 pages, 5 figures. accepted to Chem. Phys. Letters (2005

Molecular gyroscopes and biological effects of weak ELF magnetic fields

Extremely-low-frequency magnetic fields are known to affect biological systems. In many cases, biological effects display `windows' in biologically effective parameters of the magnetic fields: most dramatic is the fact that relatively intense magnetic fields sometimes do not cause appreciable effect, while smaller fields of the order of 10--100 $\mu$T do. Linear resonant physical processes do not explain frequency windows in this case. Amplitude window phenomena suggest a nonlinear physical mechanism. Such a nonlinear mechanism has been proposed recently to explain those `windows'. It considers quantum-interference effects on protein-bound substrate ions. Magnetic fields cause an interference of ion quantum states and change the probability of ion-protein dissociation. This ion-interference mechanism predicts specific magnetic-field frequency and amplitude windows within which biological effects occur. It agrees with a lot of experiments. However, according to the mechanism, the lifetime $\Gamma^{-1}$ of ion quantum states within a protein cavity should be of unrealistic value, more than 0.01 s for frequency band 10--100 Hz. In this paper, a biophysical mechanism has been proposed that (i) retains the attractive features of the ion interference mechanism and (ii) uses the principles of gyroscopic motion and removes the necessity to postulate large lifetimes. The mechanism considers dynamics of the density matrix of the molecular groups, which are attached to the walls of protein cavities by two covalent bonds, i.e., molecular gyroscopes. Numerical computations have shown almost free rotations of the molecular gyros. The relaxation time due to van der Waals forces was about 0.01 s for the cavity size of 28 angstr\"{o}ms.Comment: 10 pages, 7 figure

First-principles GW-BSE excitations in organic molecules

We present a first-principles method for the calculation of optical excitations in nanosystems. The method is based on solving the Bethe-Salpeter equation (BSE) for neutral excitations. The electron self-energy is evaluated within the GW approximation, with dynamical screening effects described within time-dependent density-functional theory in the adiabatic, local approximation. This method is applied to two systems: the benzene molecule, C$_6$H$_6$, and azobenzene, C$_{12}$H$_{10}$N$_2$. We give a description of the photoisomerization process of azobenzene after an $n-\pi^\star$ excitation, which is consistent with multi-configuration calculations