Scientific, Technical and Economic Committee for Fisheries (STECF) - Report of the STECF Study Group on the Evaluation of Fishery Multi-annual Plans (SGMOS 09-02)

SG-MOS 09-02 was held in IPIMAR, Lisbon, (Portugal), on 23-27 November 2009. The aim of the workshop was to provide Evaluations of three multiannual fisheries management plans:- R(EC) No 388/2006 ¿ multi-annual plan for sole in the Bay of Biscay; R(EC) No 209/2007 ¿ multi-annual plan for sole in the Western Channel R(EC) No676/2007 ¿ multi-annual plan for sole and plaice in the North Sea. STECF reviewed the report during its Plenary meeting on 26-30 April 2010.JRC.DG.G.4-Maritime affair

Highlights from the 6th International Society for Computational Biology Student Council Symposium at the 18th Annual International Conference on Intelligent Systems for Molecular Biology

This meeting report gives an overview of the keynote lectures and a selection of the student oral and poster presentations at the 6th International Society for Computational Biology Student Council Symposium that was held as a precursor event to the annual international conference on Intelligent Systems for Molecular Biology (ISMB). The symposium was held in Boston, MA, USA on July 9th, 2010

Scientific, Technical and Economic Committee for Fisheries (STECF)-Evaluation of Fishing Effort Regimes in European Waters Part 1 (STECF-12-09)

Informe de reunió

STECF Evaluation of Fishing Effort Regimes in European Waters - Part 2 (STECF-14-20)

DG MAR

The multiple-specificity landscape of modular peptide recognition domains

Using large scale experimental datasets, the authors show how modular protein interaction domains such as PDZ, SH3 or WW domains, frequently display unexpected multiple binding specificity. The observed multiple specificity leads to new structural insights and accurately predicts new protein interactions

Rosetta FlexPepDock ab-initio: Simultaneous Folding, Docking and Refinement of Peptides onto Their Receptors

Flexible peptides that fold upon binding to another protein molecule mediate a large number of regulatory interactions in the living cell and may provide highly specific recognition modules. We present Rosetta FlexPepDock ab-initio, a protocol for simultaneous docking and de-novo folding of peptides, starting from an approximate specification of the peptide binding site. Using the Rosetta fragments library and a coarse-grained structural representation of the peptide and the receptor, FlexPepDock ab-initio samples efficiently and simultaneously the space of possible peptide backbone conformations and rigid-body orientations over the receptor surface of a given binding site. The subsequent all-atom refinement of the coarse-grained models includes full side-chain modeling of both the receptor and the peptide, resulting in high-resolution models in which key side-chain interactions are recapitulated. The protocol was applied to a benchmark in which peptides were modeled over receptors in either their bound backbone conformations or in their free, unbound form. Near-native peptide conformations were identified in 18/26 of the bound cases and 7/14 of the unbound cases. The protocol performs well on peptides from various classes of secondary structures, including coiled peptides with unusual turns and kinks. The results presented here significantly extend the scope of state-of-the-art methods for high-resolution peptide modeling, which can now be applied to a wide variety of peptide-protein interactions where no prior information about the peptide backbone conformation is available, enabling detailed structure-based studies and manipulation of those interactions