Development of artificial neural filters for pattern recognition in protein sequences.
Four different artificial neural network architectures have been tested for their suitability to extract and predict sequence features. For optimization of the network weights an evolutionary computing method has been applied. The networks have feedforward architecture and provide adaptive neural filter systems for pattern recognition in primary structures and sequence classification. The recognition and prediction of signal peptidase cleavage sites of E. coli periplasmic protein precursors serves as an example for filter development. The primary structures are represented by seven physicochemical residue properties. This amino acid description provides the feature space for network optimization. The properties hydrophobicity, hydrophilicity, side-chain volume, and polarity allowed an accurate classification of the data. A three-layer network architecture reached a learning success of 100%; the highest prediction accuracy in an independent test set of sequences was 97%. This network architecture appears to be most suited for the analysis of E. coli signal peptidase cleavage sites. Further suggestions about the design and future applications of artificial neural networks for protein sequence analysis are made.
Schneider
G
G
Freie Universität Berlin, Fachbereich Physik, AG Biophysik, Federal Republic of Germany.
Wrede
P
P
D001426:Bacterial Proteins / Q000737:chemistry; D005075:Biological Evolution; D016208:Databases, Factual; D004926:Escherichia coli / Q000235:genetics; D016571:Neural Networks, Computer; D011498:Protein Precursors / Q000737:chemistry; D021382:Protein Sorting Signals / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D011498:Protein Precursors; D021382:Protein Sorting Signals; D011506:Proteins