Discarge compilation from The Global River Discharge (RivDIS) Project

The Global River Discharge (RivDIS) data set contains monthly discharge measurements for 1018 stations located throughout the world. The period of record varies widely from station to station, with a mean of 21.5 years. These data were digitized from published UNESCO archives by Charles Voromarty, Balaze Fekete, and B.A. Tucker of the Complex Systems Research Center (CSRC) at the University of New Hampshire. River discharge is typically measured through the use of a rating curve that relates local water level height to discharge. This rating curve is used to estimate discharge from the observed water level. The rating curves are periodically rechecked and recalibrated through on-site measurement of discharge and river stage.

Quinta pars huius operis co[n]tine[n]s postillam / d[omi]ni Hugonis Cardinalis super quattuor eua[n]gelia s[e]c[un]d[u]m Mattheu[m], Marcum, Lucam, Iohannem.

Sign.: a8, b6, c8, d6, e8, f6, g8, h6, i8, k6, l8, m6, n8, o6, p8, q6, r8, s6, t8, u6, x8, y6, z8, A6, B8, C6, D8, E6, F8, G6, H8, I6, K8, L6, M8, N6, O8, P6, Q8, R6, S8, T6, U8, X6, Y8, Z6, 2A8, 2B6, 2C8, 2D-2F6

Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA

The capsid protein of hepatitis B virus, consisting of an “assembly” domain (residues 1–149) and an RNA-binding “protamine” domain (residues 150–183), assembles from dimers into icosahedral capsids of two different sizes. The C terminus of the assembly domain (residues 140–149) functions as a morphogenetic switch, longer C termini favoring a higher proportion of the larger capsids, it also connects the protamine domain to the capsid shell. We now have defined the location of this peptide in capsids assembled in vitro by engineering a mutant assembly domain with a single cysteine at its C terminus (residue 150), labeling it with a gold cluster and visualizing the cluster by cryo-electron microscopy. The labeled protein is unimpaired in its ability to form capsids. Our density map reveals a single undecagold cluster under each fivefold and quasi-sixfold vertex, connected to sites at either end of the undersides of the dimers. Considering the geometry of the vertices, the C termini must be more crowded at the fivefolds. Thus, a bulky C terminus would be expected to favor formation of the larger (T = 4) capsids, which have a greater proportion of quasi-sixfolds. Capsids assembled by expressing the full-length protein in Escherichia coli package bacterial RNAs in amounts equivalent to the viral pregenome. Our density map of these capsids reveals a distinct inner shell of density—the RNA. The RNA is connected to the protein shell via the C-terminal linkers and also makes contact around the dimer axes.

Red de coordinación y seguimiento del primer curso del Grado en Ing. Sonido e Imagen en Telecomunicación (GISIT) de la Escuela Politécnica Superior

El profesorado de la red docente durante el curso 2011/12 ha realizado un proyecto coordinar las las asignaturas del primer curso del Grado en Ingeniería en Sonido e Imagen en Telecomunicación de la Escuela Politécnica Superior. Se ha realizado una puesta en común con los coordinadores de todos los cursos para realizar las recomendaciones de matriculación a los estudiantes que realizan su matricula a tiempo parcial o no superan cada curso todos los créditos matriculados. Se ha realizado un ajuste de los temarios con las asignaturas que comienzan su implantación en el siguiente curso y por otro lado una coordinación en la evaluación para eliminar las numerosas coincidencias de evaluaciones continuas, de diferentes actividades en cada semana.