On vanishing sums of m \,m\,th roots of unity in finite fields

In an earlier work, the authors have determined all possible weights $n$ for which there exists a vanishing sum $\zeta_1+\cdots +\zeta_n=0$ of $m$th roots of unity $\zeta_i$ in characteristic 0. In this paper, the same problem is studied in finite fields of characteristic $p$. For given $m$ and $p$, results are obtained on integers $n_0$ such that all integers $n\geq n_0$ are in the ``weight set'' $W_p(m)$. The main result $(1.3)$ in this paper guarantees, under suitable conditions, the existence of solutions of $x_1^d+\cdots+x_n^d=0$ with all coordinates not equal to zero over a finite field

Elementary Proofs Of Two Theorems Involving Arguments Of Eigenvalues Of A Product Of Two Unitary Matrices

We give elementary proofs of two theorems concerning bounds on the maximum argument of the eigenvalues of a product of two unitary matrices --- one by Childs \emph{et al.} [J. Mod. Phys., \textbf{47}, 155 (2000)] and the other one by Chau [arXiv:1006.3614]. Our proofs have the advantages that the necessary and sufficient conditions for equalities are apparent and that they can be readily generalized to the case of infinite-dimensional unitary operators.Comment: 8 pages in Revtex 4.1 preprint format, to appear in Journal of Inequalities and Application

Hybrid biomedical intelligent systems

"Copyright © 2012 Maysam Abbod et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited."The purpose of this special issue is to promote research and developments of the best work in the field of hybrid intelligent systems for biomedical applications

Ligand-biased ensemble receptor docking (LigBEnD): a hybrid ligand/receptor structure-based approach.

Ligand docking to flexible protein molecules can be efficiently carried out through ensemble docking to multiple protein conformations, either from experimental X-ray structures or from in silico simulations. The success of ensemble docking often requires the careful selection of complementary protein conformations, through docking and scoring of known co-crystallized ligands. False positives, in which a ligand in a wrong pose achieves a better docking score than that of native pose, arise as additional protein conformations are added. In the current study, we developed a new ligand-biased ensemble receptor docking method and composite scoring function which combine the use of ligand-based atomic property field (APF) method with receptor structure-based docking. This method helps us to correctly dock 30 out of 36 ligands presented by the D3R docking challenge. For the six mis-docked ligands, the cognate receptor structures prove to be too different from the 40 available experimental Pocketome conformations used for docking and could be identified only by receptor sampling beyond experimentally explored conformational subspace

Origin of Discrepancies in Inelastic Electron Tunneling Spectra of Molecular Junctions

We report inelastic electron tunneling spectroscopy (IETS) of multilayer molecular junctions with and without incorporated metal nano-particles. The incorporation of metal nanoparticles into our devices leads to enhanced IET intensity and a modified line-shape for some vibrational modes. The enhancement and line-shape modification are both the result of a low lying hybrid metal nanoparticle-molecule electronic level. These observations explain the apparent discrepancy between earlier IETS measurements of alkane thiolate junctions by Kushmerick \emph{et al.} [Nano Lett. \textbf{4}, 639 (2004)] and Wang \emph{et al.} [Nano Lett. \textbf{4}, 643 (2004)].Comment: 4 pages, 4 figures accepted for publication in Physical Review Letter