Solar Neutrinos as Background to Neutrinoless Double-beta Decay Experiments

Solar neutrinos interact within double-beta decay (\BB) detectors and contribute to backgrounds for \BB\ experiments. Background contributions due to charge-current solar neutrino interactions with \BB\ nuclei of $^{76}$Ge, $^{82}$Se, $^{100}$Mo, $^{130}$Te, $^{136}$Xe, and $^{150}$Nd are evaluated. They are shown to be significant for future high-sensitivity \BB\ experiments that may search for Majorana neutrino masses in the inverted-hierarchy mass region. The impact of solar neutrino backgrounds and their reduction are discussed for future \BB\ experiments.Comment: proceedings submission for MEDEX 201

Possible Lattice Distortions in the Hubbard Model for Graphene

The Hubbard model on the honeycomb lattice is a well known model for graphene. Equally well known is the Peierls type of instability of the lattice bond lengths. In the context of these two approximations we ask and answer the question of the possible lattice distortions for graphene in zero magnetic field. The answer is that in the thermodynamic limit only periodic, reflection-symmetric distortions are allowed and these have at most six atoms per unit cell as compared to two atoms for the undistorted lattice.Comment: 5 pages, 3 figure

Crystal structure of Schmallenberg orthobunyavirus nucleoprotein-RNA complex reveals a novel RNA sequestration mechanism

Schmallenberg virus (SBV) is a newly emerged orthobunyavirus (family Bunyaviridae) that has caused severe disease in the offspring of farm animals across Europe. Like all orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that is encapsidated by the viral nucleocapsid (N) protein in the form of a ribonucleoprotein complex (RNP). We recently reported the three-dimensional structure of SBV N that revealed a novel fold. Here we report the crystal structure of the SBV N protein in complex with a 42-nt-long RNA to 2.16 Å resolution. The complex comprises a tetramer of N that encapsidates the RNA as a cross-shape inside the protein ring structure, with each protomer bound to 11 ribonucleotides. Eight bases are bound in the positively charged cleft between the N- and C-terminal domains of N, and three bases are shielded by the extended N-terminal arm. SBV N appears to sequester RNA using a different mechanism compared with the nucleoproteins of other negative-sense RNA viruses. Furthermore, the structure suggests that RNA binding results in conformational changes of some residues in the RNA-binding cleft and the N- and C-terminal arms. Our results provide new insights into the novel mechanism of RNA encapsidation by orthobunyaviruses

Study of low gravity propellant transfer Quarterly progress report, 23 Dec. 1970 - 30 Apr. 1971

Bellows, metallic diaphragm, and paddle vortex subcritical transfer systems designs and high pressure systems analyses for orbital space station cryogen