East European Journal of Physics

5

Authors: A. Yu. Buki, I. S. Timchenko

The new experimental Coulomb sums values of 6Li and 7Li nuclei have been obtained at momentum transfers range q = 0.750¸ 1.000 fm-1 and q = 0.750¸ 1.125 fm-1, respectively, extending significantly the earlier reported momentum transfers range of Coulomb sums for these nuclei. The dependence of the 6Li and 7Li Coulomb sums on the momentum transferred is shown to differ substantially from same dependences for all the other investigated nuclei. It is suggested that the observed feature of the 6Li and 7Li Coulomb sums is related to a strong clusterization of these nuclei. The parameter qp corresponding to the value of the momentum transferred, at which the Coulomb sum ceases to grow and remains constant for larger momentum transfers, is introduced. The values of the parameter qp for the lithium isotopes nuclei were obtained (qp(7Li) = 1.20 ± 0.10fm-1 and qp(7Li) = 1.35 ± 0.10 fm-1), which are much lower than qp of 4He, 12C, 40Ca, 48Ca and 56Fe nuclei (qp » 2 fm-1). The graph represented the qp values of the nuclei as a function of the isolation parameter x, which characterizing the degree of nuclear clusterization, is constructed. The obtained graph shows the explicit proportionality of the qp dependence from the parameter x and predicts the qp value for the Coulomb sum of the 9Be nucleus not yet measured.

6

Authors: N. Yu. Filonenko

EAST EUROPEAN JOURNAL OF PHYSICS OPEN JOURNAL SYSTEMS Journal Help USER You are logged in as... hirnyk My Journals My Profile Log Out NOTIFICATIONS View (125 new) Manage LANGUAGE Select Language JOURNAL CONTENT Search Search Scope Browse By Issue By Author By Title Other Journals Categories FONT SIZE Make font size smallerMake font size defaultMake font size larger ARTICLE TOOLS Print this article Indexing metadata How to cite item Finding References Review policy Email this article Email the author KEYWORDS NEMUS spectrometer on Bonner spheres X-ray analysis X-ray diffraction alloys amyloid fibrils computer simulation convergence of integrals defects differential equations dislocations generations of particles heat capacity ionoluminescence lysozyme magnetic field neutron radiation spectrum phases segregation storage ring thermodynamic functions zirconium HOME ABOUT USER HOME CATEGORIES SEARCH CURRENT ARCHIVES ANNOUNCEMENTS STATISTICS Home > Vol 1, No 1 (2018) > Filonenko THERMODYNAMICS AND STRUCTURAL CONDITION OF PB-SB ALLOYS N. Yu. Filonenko ABSTRACT In this paper we study the structural condition and thermodynamic functions of a melt of the Pb-Sb. The investigations were performed for alloys with an antimony content of 5.0-20.0% (wt.), the rest is lead. To determine the structural condition of alloys we use microstructure analysis, differential thermal and X-ray structural analyses. The phase composition of alloys was determined in relation to the temperature of the liquid heating above the liquidus curve and to the cooling rate. With accounting for the first degree approximation of high-temperature expansion of the thermodynamic potential in expression for the Gibbs energy of a melt of the binary Pb-Sb alloy we find the curve of thermodynamic stability of the liquid depending on the antimony content in alloy. This approach enables to give the most complete description of the alloys’ melt from the thermodynamic point of view and to determine a thermodynamic stability curve, above which there are no microcomplexes in the phase. The results of the calculations obtained in this paper are in good agreement with the experimental data

8

Authors: V. Trusova, G. Gorbenko

Intermolecular noncovalent interactions between protein molecules result in the formation of a wide spectrum of supramolecular assemblies the structure of which varies from disordered amorphous aggregates to the crystals with strictly defined translational symmetry in three directions. One-dimensional protein aggregates (amyloid fibrils) represent highly ordered semiflexible polymers with unique mesoscopic properties which can be tuned by both intrinsic physicochemical characteristics of polypeptide chain and milieu conditions. In the present work the molecular mechanisms of amyloid formation are discussed and mathematical description of the existing models of protein fibrillization are given. For disease-related amyloids, deeper understanding of fibril growth process may shed light on the pathogenesis and molecular mechanisms of the disorders, as well as on the strategies of amyloidosis prevention at atomistic level. In the context of nanotechnology and functional material science, knowing the details of amyloid formation is crucially required for the design of novel nanomaterials with unprecedented qualities.

11

Authors: D. O. Vasylenko, V. S. Sydorenko, P. O. Kravchuk, V. I. Grygoruk, V. I. Kanevskii

In this paper, we propose a model of a dipole with an atomic structure instead of the standard dipole model with point unlike charges and the Hertzian dipole model, which have significant drawbacks. The equations of the Hertzian dipole and the standard model operate from a distance much larger than size of the dipole, and the quasistatic Coulomb and Biot-Savart fields are the essence of the reactive near field, its own fields with a phase shift ΔφE,H = π/2, which have no restrictions on the distances to a dipole, since they are directly related to charges and their motion – currents. In the framework of the proposed dipole model, we described the physical mechanisms for the formation of near and far fields of an oscillating dipole, which are based on the use of the Coulomb and Biot-Savart fields, the quasistatic lines of force of their electric charge fields Е, and the magnetic fields of the currents Н for the analysis of energy fluxes: reactive Sr at ΔφE,H = π/2 and active Sа at ΔφE,H = 0 alike.