MEASURING THE WAVE DISSIPATION PRODUCED BY A SWIMMING-LINE SEPARATION ROPE

Hydrodynamic drag (D) seems to be one of the major determinants of swimming performance. D is usually divided into pressure, friction and wave drag (Dw). Meanwhile, Dw can be due to two distinct phenomena: (i) wave production (Dwwp) and (ii) transfer of negative wave momentum (Dwtm). Dwwp refers to the energy dissipated from the kinetic energy of the swimmer and used to generate waves, and Dwtm refers to the drag effect (reduction of forward kinetic energy of the swimmer) attributed to the impact of waves produced by others, or produced by the swimmer itself and rebounded at a swimming pool wall. In order to define the competition lane of each swimmer, the competition swimming pools dispose of swimming-line separation ropes (S-LSR). In the meantime, the manufacturers of this S-LSR claim that they have the ability to absorb waving energy, and thus to dissipate waves avoiding Dw tm, and other perturbing wave effects. The purpose of this research was to characterize the swimmer’s wave production, and to measure the effect upon the wave energy dissipation of a common S-LSR (Fig.1)

Pfam: clans, web tools and services

Pfam is a database of protein families that currently contains 7973 entries (release 18.0). A recent development in Pfam has enabled the grouping of related families into clans. Pfam clans are described in detail, together with the new associated web pages. Improvements to the range of Pfam web tools and the first set of Pfam web services that allow programmatic access to the database and associated tools are also presented. Pfam is available on the web in the UK (http://www.sanger.ac.uk/Software/Pfam/), the USA (http://pfam.wustl.edu/), France (http://pfam.jouy.inra.fr/) and Sweden (http://pfam.cgb.ki.se/)

Pfam: the protein families database

Peer reviewe

Predicting active site residue annotations in the Pfam database

<p>Abstract</p> <p>Background</p> <p>Approximately 5% of Pfam families are enzymatic, but only a small fraction of the sequences within these families (<0.5%) have had the residues responsible for catalysis determined. To increase the active site annotations in the Pfam database, we have developed a strict set of rules, chosen to reduce the rate of false positives, which enable the transfer of experimentally determined active site residue data to other sequences within the same Pfam family.</p> <p>Description</p> <p>We have created a large database of predicted active site residues. On comparing our active site predictions to those found in UniProtKB, Catalytic Site Atlas, PROSITE and <it>MEROPS </it>we find that we make many novel predictions. On investigating the small subset of predictions made by these databases that are not predicted by us, we found these sequences did not meet our strict criteria for prediction. We assessed the sensitivity and specificity of our methodology and estimate that only 3% of our predicted sequences are false positives.</p> <p>Conclusion</p> <p>We have predicted 606110 active site residues, of which 94% are not found in UniProtKB, and have increased the active site annotations in Pfam by more than 200 fold. Although implemented for Pfam, the tool we have developed for transferring the data can be applied to any alignment with associated experimental active site data and is available for download. Our active site predictions are re-calculated at each Pfam release to ensure they are comprehensive and up to date. They provide one of the largest available databases of active site annotation.</p

The Pfam protein families database

Peer reviewe

The Pfam protein families database

Peer reviewe