Molecular Barcoding of Eupatorieae of Tennessee

Molecular analysis has become a popular method used to characterize the complex biodiversity of our world. In this project, we have been able to add to the understanding of the native species of Tennessee by analyzing particular regions of DNA. We obtained DNA sequences for a standard barcode marker from each of about 30 species belonging to the Eupatorieae tribe found in the state. This process of molecular barcoding has produced a catalog of the state’s diversity of these plants. With this, we are better able to identify unknown samples and aid in the conservation of rare plants such as Eupatorium leucolepis. This plant, also known as justiceweed, is a flowering plant currently listed as endangered in the state of Tennessee. While commonly found in the coastal plain region, justiceweed is also native to one county in Tennessee. Isolated by hundreds of miles from any other of its species, the populations of this plant found in Tennessee have raised some questions. Is this truly the same plant that grows along the eastern coast of North America? If so how did it come to occupy this land locked state? So far, we have been unable to find a characteristic to distinguish Tennessee’s justiceweed from that of coastal plain populations. However, molecular data have determined that the plants in Tennessee previously identified as E. leucolepis differ significantly from those found in the coastal plain region, and instead are hybrids of E. leucolepis and E. semiserratum, a species more commonly found in Tennessee

Understanding micro-image configurations in quasar microlensing

The micro-arcsecond scale structure of the seemingly point-like images in lensed quasars, though unobservable, is nevertheless much studied theoretically, because it affects the observable (or macro) brightness, and through that provides clues to substructure in both source and lens. A curious feature is that, while an observable macro-image is made up of a very large number of micro-images, the macro flux is dominated by a few micro-images. Micro minima play a key role, and the well-known broad distribution of macro magnification can be decomposed into narrower distributions with 0,1,2,3,... micro minima. This paper shows how the dominant micro-images exist alongside the others, using the ideas of Fermat's principle and arrival-time surfaces, alongside simulations.Comment: Accepted for publication in MNRA

Electronic shielding by closed shells in salts of thulium

Electronic shielding by closed electron shells has been investigated in salts of trivalent thulium, by measuring the temperature dependence of the nuclear quadrupole splitting of the 8.42-keV gamma transition in Tm169. The measurements were performed by using the technique of recoilless nuclear resonance absorption. The nuclear quadrupole interaction was studied for Tm3+ ions in thulium ethyl sulfate, thulium oxide, and thulium trifluoride within a temperature range from 9.6 to 1970°K. The interpretation of the experimental data in terms of the contributions of distorted closed electron shells to the quadrupole interaction yields values for electronic shielding factors. The results lead to amounts of 10% or less for the atomic Sternheimer factor RQ. The experiments also reveal substantial shielding of the 4f electrons from the crystal electric field, expressed by the shielding factor σ2. Values of 250 and 130 are obtained for the ratio (1-γ∞)/(1-σ2) for thulium ethyl sulfate and thulium oxide, respectively, where γ∞ is the lattice Sternheimer factor

Alternative mechanism for bacteriophage adsorption to the motile bacterium Caulobacter crescentus

2D and 3D cryo-electron microscopy, together with adsorption kinetics assays of ϕCb13 and ϕCbK phage-infected Caulobacter crescentus, provides insight into the mechanisms of infection. ϕCb13 and ϕCbK actively interact with the flagellum and subsequently attach to receptors on the cell pole. We present evidence that the first interaction of the phage with the bacterial flagellum takes place through a filament on the phage head. This contact with the flagellum facilitates concentration of phage particles around the receptor (i.e., the pilus portals) on the bacterial cell surface, thereby increasing the likelihood of infection. Phage head filaments have not been well characterized and their function is described here. Phage head filaments may systematically underlie the initial interactions of phages with their hosts in other systems and possibly represent a widespread mechanism of efficient phage propagation

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB

AbstractBackground: Human thioredoxin is a 12 kDa cellular redox protein that plays a key role in maintaining the redox environment of the cell. It has recently been shown to be responsible for activating the DNA-binding properties of the cellular transcription factor, NFκB, by reducing a disulfide bond involving Cys62 of the p50 subunit. Using multidimensional heteronuclear-edited and heteronuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56–68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway.Results The NFκB peptide is located in a long boot-shaped cleft on the surface of human thioredoxin delineated by the active-site loop, helices α2, α3 and α4, and strands β3 and β4. The peptide adopts a crescent-like conformation with a smooth 110° bend centered around residue 60 which permits it to follow the path of the cleft.Conclusion In addition to the intermolecular disulfide bridge between Cys32 of human thioredoxin and Cys62 of the peptide, the complex is stabilized by numerous hydrogen-bonding, electrostatic and hydrophobic interactions which involve residues 57–65 of the NFκB peptide and confer substrate specificity. These structural features permit one to suggest the specificity requirements for human thioredoxin-catalyzed disulfide bond reduction of proteins