Quantum simulation of topologically protected states using directionally unbiased linear-optical multiports

It is shown that quantum walks on one-dimensional arrays of special linear-optical units allow the simulation of discrete-time Hamiltonian systems with distinct topological phases. In particular, a slightly modified version of the Su-Schrieffer-Heeger (SSH) system can be simulated, which exhibits states of nonzero winding number and has topologically protected boundary states. In the large-system limit this approach uses quadratically fewer resources to carry out quantum simulations than previous linear-optical approaches and can be readily generalized to higher-dimensional systems. The basic optical units that implement this simulation consist of combinations of optical multiports that allow photons to reverse direction

Quantum simulation of discrete-time Hamiltonians using directionally unbiased linear optical multiports

Recently, a generalization of the standard optical multiport was proposed [Phys. Rev. A 93, 043845 (2016)]. These directionally unbiased multiports allow photons to reverse direction and exit backwards from the input port, providing a realistic linear optical scattering vertex for quantum walks on arbitrary graph structures. Here, it is shown that arrays of these multiports allow the simulation of a range of discrete-time Hamiltonian systems. Examples are described, including a case where both spatial and internal degrees of freedom are simulated. Because input ports also double as output ports, there is substantial savings of resources compared to feed-forward networks carrying out the same functions. The simulation is implemented in a scalable manner using only linear optics, and can be generalized to higher dimensional systems in a straightforward fashion, thus offering a concrete experimentally achievable implementation of graphical models of discrete-time quantum systems.This research was supported by the National Science Foundation EFRI-ACQUIRE Grant No. ECCS-1640968, NSF Grant No. ECCS-1309209, and by the Northrop Grumman NG Next. (ECCS-1640968 - National Science Foundation EFRI-ACQUIRE Grant; ECCS-1309209 - NSF Grant; Northrop Grumman NG Next

Sum rules of codon usage probabilities

In the crystal basis model of the genetic code, it is deduced that the sum of usage probabilities of the codons with C and A in the third position for the quartets and/or sextets is independent of the biological species for vertebrates. A comparison with experimental data shows that the prediction is satisfied within about 5 %.Comment: 7 page

Fetus in Fetu: A Case Report and Review of Literature

Fetus-in-fetu is a rare congenital malformation in which a vertebra fetus is enclosed within the abdomen of a normally developing fetus. The preoperative diagnosis is challenging. Less than 200 cases are reported in English literature, five in Africa. Multiple fetuses-in-fetu are less documented. We report a three month old infant who presented with an abdominal mass and constipation and taken to theatre with a preoperative diagnosis of a teratoma. At operation, the mass was a case of twin fetuses in fetu with blood supply from the aorta and the left renal artery. Total excision of the mass with special attention to its blood supply was therapeutic. We emphasize the necessity for suspicion of fetus in fetu when a well-defined encapsulated cystic mass with calcified solid components is detected by an abdominal CT scan in a child less than 2 years of age. The Annals of African Surgery, Volume 6, 201

Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins

FtsZ, a bacterial tubulin homologue, is a cytoskeletal protein that assembles into protofilaments that are one subunit thick. These protofilaments assemble further to form a “Z ring” at the center of prokaryotic cells. The Z ring generates a constriction force on the inner membrane and also serves as a scaffold to recruit cell wall remodeling proteins for complete cell division in vivo. One model of the Z ring proposes that protofilaments associate via lateral bonds to form ribbons; however, lateral bonds are still only hypothetical. To explore potential lateral bonding sites, we probed the surface of Escherichia coli FtsZ by inserting either small peptides or whole fluorescent proteins (FPs). Among the four lateral surfaces on FtsZ protofilaments, we obtained inserts on the front and back surfaces that were functional for cell division. We concluded that these faces are not sites of essential interactions. Inserts at two sites, G124 and R174, located on the left and right surfaces, completely blocked function, and these sites were identified as possible sites for essential lateral interactions. However, the insert at R174 did not interfere with association of protofilaments into sheets and bundles in vitro. Another goal was to find a location within FtsZ that supported insertion of FP reporter proteins while allowing the FtsZ-FPs to function as the sole source of FtsZ. We discovered one internal site, G55-Q56, where several different FPs could be inserted without impairing function. These FtsZ-FPs may provide advances for imaging Z-ring structure by superresolution techniques. IMPORTANCE One model for the Z-ring structure proposes that protofilaments are assembled into ribbons by lateral bonds between FtsZ subunits. Our study excluded the involvement of the front and back faces of the protofilament in essential interactions in vivo but pointed to two potential lateral bond sites, on the right and left sides. We also identified an FtsZ loop where various fluorescent proteins could be inserted without blocking function; these FtsZ-FPs functioned as the sole source of FtsZ. This advance provides improved tools for all fluorescence imaging of the Z ring and may be especially important for superresolution imaging

Electrooxidation of formic acid on gold : An ATR-SEIRAS study of the role of adsorbed formate

Funding from the DGI (Spanish Ministry of Education and Science) through Projects CTQ2009-07017 and PLE2009-0008 is gratefully acknowledged. M.E.-E. acknowledges an FPI fellowship from the Spanish Ministry of Science and Innovation and an accommodation grant at the Residencia de Estudiantes from the Madrid City Council. C. V.-D. acknowledges a JAE-Doc fellowship from CSIC.Peer reviewedPostprin