SOPMA - SIGNIFICANT IMPROVEMENTS IN PROTEIN SECONDARY STRUCTURE PREDICTION BY CONSENSUS PREDICTION FROM MULTIPLE ALIGNMENTS

Recently a new method called the self-optimized prediction method (SOP M) has been described to improve the success rate in the prediction of the secondary structure of proteins. rn this paper we report improvem ents brought about by predicting all the sequences of a set of aligned proteins belonging to the same family. This improved SOPM method (SOP MA) correctly predicts 69.5% of amino acids for a three-state descript ion of the secondary structure (alpha-helix, beta-sheet and coil) in a whole database containing 126 chains of non-homologous (less than 25% identity) proteins. Joint prediction with SOPMA and a neural networks method (PHD) correctly predicts 82.2% of residues for 74% of co-predi cted amino acids. Predictions are available by Email to deleage@ibcp.f r or on a Web page (http://www.ibcp,fl/predict.html).