A comparison of the performance of Kalpana and Meteosat-7 WV radiances in the ECMWF NWP model

The Kalpana Very High Resolution Radiometer (VHRR) water vapour (WV) channel is very similar to the WV channel of the Meteosat Visible and Infrared Radiation Imager (MVIRI) on Meteosat-7, and both satellites observe the Indian subcontinent. Thus it is possible to compare the performance of VHRR and MVIRI in numerical weather prediction (NWP) models. In order to do so, the impact of Kalpana- and Meteosat-7-measured WV radiances was evaluated using analyses and forecasts of moisture, temperature, geopotential and winds, using the European Centre for Medium-range Weather Forecasts (ECMWF) NWP model. Compared with experiments using Meteosat-7, the experiments using Kalpana WV radiances show a similar fit to all observations and produce very similar forecasts.

Phage display selection of ligand residues important for Src homology 3 domain binding specificity.

The Src homology 3 (SH3) domain is a 50-aa modular unit present in many cellular proteins involved in intracellular signal transduction. It functions to direct protein-protein interactions through the recognition of proline-rich motifs on associated proteins. SH3 domains are important regulatory elements that have been demonstrated to specify distinct regulatory pathways important for cell growth, migration, differentiation, and responses to the external milieu. By the use of synthetic peptides, ligands have been shown to consist of a minimum core sequence and to bind to SH3 domains in one of two pseudosymmetrical orientations, class I and class II. The class I sites have the consensus sequence ZP(L/P)PP psi P whereas the class II consensus is PP psi PPZ (where psi is a hydrophobic residue and Z is a SH3 domain-specific residue). We previously showed by M13 phage display that the Src, Fyn, Lyn, and phosphatidylinositol 3-kinase (PI3K) SH3 domains preferred the same class I-type core binding sequence, RPLPP psi P. These results failed to explain the specificity for cellular proteins displayed by SH3 domains in cells. In the current study, class I and class II core ligand sequences were displayed on the surface of bacteriophage M13 with five random residues placed either N- or C-terminal of core ligand residues. These libraries were screened for binding to the Src, Fyn, Lyn, Yes, and PI3K SH3 domains. By this approach, additional ligand residue preferences were identified that can increase the affinity of SH3 peptide ligands at least 20-fold compared with core peptides. The amino acids selected in the flanking sequences were similar for Src, Fyn, and Yes SH3 domains; however, Lyn and PI3K SH3 domains showed distinct binding specificities. These results indicate that residues that flank the core binding sequences shared by many SH3 domains are important determinants of SH3 binding affinity and selectivity.

The crack of doom.

Mode of access: Internet.

Cobro coercitivo de deudas públicas /

Filmed from the original held by: Bibliotheek, Vredespaleis, Den Haag.

The Bamberg rider; studies of mediaeval German sculpture.

Mode of access: Internet.

The recipe for rubber : a Fijian romance /

Illustrated by Norman Lindsay.

Catalogus codicum orientalium Bibliothecae Academiae Lugduno Batavae auctore R. P. A. Dozy ...

Vol. 6, "Pars prior." No more published?

Lijst van aanwinsten.

At head of title: Universiteitsbibliotheek van Amsterdam (1917-22, Bibliotheek der Universiteit...)

Catalogus bibliothecae Amstelredamensis. Lugduni Batavorum, 1612.

Mode of access: Internet.

Mededelingen Landbouwhogeschool Wageningen, Nederland.

Mode of access: Internet.

Catalogus van de bibliotheken der Maatschappij tot bevordering der toonkunst en der Vereeniging voor Noord-Nederlands muziekgeschiedenis.

Preface signed: H. C. Rogge.

New æra : a socialist romance : with a chapter on vaccination /

Mode of access: Internet.

Catalogus der geschiedenis ...

Mode of access: Internet.

Pharos, the Egyptian;

Mode of access: Internet.