Scaling of human behavior during portal browsing

We investigate transitions of portals users between different subpages. A weighted network of portals subpages is reconstructed where edge weights are numbers of corresponding transitions. Distributions of link weights and node strengths follow power laws over several decades. Node strength increases faster than linearly with node degree. The distribution of time spent by the user at one subpage decays as power law with exponent around 1.3. Distribution of numbers P(z) of unique subpages during one visit is exponential. We find a square root dependence between the average z and the total number of transitions n during a single visit. Individual path of portal user resembles of self-attracting walk on the weighted network. Analytical model is developed to recover in part the collected data.Comment: 6 pages, 7 figure

Nuclear spins, magnetic moments and quadrupole moments of Cu isotopes from N = 28 to N = 46: probes for core polarization effects

Measurements of the ground-state nuclear spins, magnetic and quadrupole moments of the copper isotopes from 61Cu up to 75Cu are reported. The experiments were performed at the ISOLDE facility, using the technique of collinear laser spectroscopy. The trend in the magnetic moments between the N=28 and N=50 shell closures is reasonably reproduced by large-scale shell-model calculations starting from a 56Ni core. The quadrupole moments reveal a strong polarization of the underlying Ni core when the neutron shell is opened, which is however strongly reduced at N=40 due to the parity change between the $pf$ and $g$ orbits. No enhanced core polarization is seen beyond N=40. Deviations between measured and calculated moments are attributed to the softness of the 56Ni core and weakening of the Z=28 and N=28 shell gaps.Comment: 13 pagers, 19 figures, accepted by Physical Review

Chemical composition of atherosclerotic plaques of apoE/LDLR-double knockout mice by synchrotron radiation FTIR microspectroscopy

Atherosclerosis is a multietiological inflammatory disease of large and medium-sized arteries of increasing incidence in westernized countries. The aim of this study was to identify the biochemical changes during the progression of atherosclerosis by synchrotron radiation Fourier transform infrared microspectroscopy in atheromas of apoE/$LDLR^{-//-}$ mice fed egg-rich diet supplemented or not with angiotensin converting enzyme inhibitor perindopril. Synchrotron radiation Fourier transform infrared microspectroscopy technique was used to obtain information at high spatial resolution about the distribution of proteins (C-N, N-H, CO for amide I and amide II bands), lipids ($CH_2$, $CH_3$ bands) as well as mineral deposits (calcium carbonates and phosphates). Total contents of lipids and proteins were found to be significantly lower in animals treated with the diet and perindopril. An increase in saturation level of lipids was observed in animals fed with egg-rich diet when compared to the normal diet and perindopril treatment, which did not inhibit this effect. Moreover, a significant change in the secondary structure of proteins (ratio between absorption bands 1634 $cm^{-1}$/1656 $cm^{-1}$ attributed to β-type and α-type, respectively) was observed in both experimental groups in comparison with the control. Principal component analysis was used to analyse the recorded spectra. It has revealed that higher content of phosphates (wavenumber range 950-1020 $cm^{-1}$) was observed between egg-rich diet fed animals and the control group

Probing the N = 32 shell closure below the magic proton number Z = 20: Mass measurements of the exotic isotopes 52,53K

The recently confirmed neutron-shell closure at N = 32 has been investigated for the first time below the magic proton number Z = 20 with mass measurements of the exotic isotopes 52,53K, the latter being the shortest-lived nuclide investigated at the online mass spectrometer ISOLTRAP. The resulting two-neutron separation energies reveal a 3 MeV shell gap at N = 32, slightly lower than for 52Ca, highlighting the doubly-magic nature of this nuclide. Skyrme-Hartree-Fock-Boguliubov and ab initio Gorkov-Green function calculations are challenged by the new measurements but reproduce qualitatively the observed shell effect.Comment: 5 pages, 5 figure

RGD-containing Peptides Inhibit Fibrinogen Binding to Platelet αIIbβ3 by Inducing an Allosteric Change in the Amino-terminal Portion of αIIb

To determine the molecular basis for the insensitivity of rat alpha(IIb)beta(3) to inhibition by RGD-containing peptides, hybrids of human and rat alpha(IIb)beta(3) and chimeras of alpha(IIb)beta(3) in which alpha(IIb) was composed of portions of human and rat alpha(IIb) were expressed in Chinese hamster ovary cells and B lymphocytes, and the ability of the tetrapeptide RGDS to inhibit fibrinogen binding to the various forms of alpha(IIb)beta(3) was measured. These measurements indicated that sequences regulating the sensitivity of alpha(IIb)beta(3) to RGDS are located in the seven amino-terminal repeats of alpha(IIb). Moreover, replacing the first three or four (but not the first two) repeats of rat alpha(IIb) with the corresponding human sequences enhanced sensitivity to RGDS, whereas replacing the first two or three repeats of human alpha(IIb) with the corresponding rat sequences had little or no effect. Nevertheless, RGDS bound to Chinese hamster ovary cells expressing alpha(IIb)beta(3) regardless whether the alpha(IIb) in the heterodimers was human, rat, or a rat-human chimera. These results indicate that the sequences determining the sensitivity of alpha(IIb)beta(3) to RGD-containing peptides are located in the third and fourth amino-terminal repeats of alpha(IIb). Because RGDS binds to both human and rat alpha(IIb)beta(3), the results suggest that differences in RGDS sensitivity result from differences in the allosteric changes induced in these repeats following RGDS binding