Predicting alpha-helix and beta-strand segments of globular proteins.

All current methods of protein secondary structure prediction are based on evaluation of a single residue state. Although the accuracy of the best of them is approximately 60-70%, for reliable prediction of tertiary structure it is more useful to predict an approximate location of alpha-helix and beta-strand segments, especially prolonged ones. We have developed a simple method for protein secondary structure prediction which is oriented on the location of secondary structure segments. The method uses linear discriminant analysis to assign segments of a given amino acid sequence a particular type of secondary structure, by taking into account the amino acid composition of internal parts of segments as well as their terminal and adjacent regions. Four linear discriminant functions were constructed for recognition of short and long alpha-helix and beta-strand segments respectively. These functions combine three characteristics: hydrophobic moment, segment singlet, and pair preferences to an alpha-helix or beta-strand. The last two characteristics are calculated by summing the preference parameters of single residues and pairs of residues located in a segment and its adjacent regions. The final program SSP predicts all possible potential alpha-helices and beta-strands and resolves some possible overlap between them. Overall three-state (alpha, beta, c) prediction gives approximately 65.1% correctly predicted residues on 126 non-homologous proteins using the jackknife test procedure. Analysis of the prediction results shows a high prediction accuracy of long secondary structure segments (approximately 89% of alpha-helices of length > 8 and approximately 71% of beta-strands of length > 6 are correctly located with probability of correct prediction 0.82 and 0.78 respectively.(ABSTRACT TRUNCATED AT 250 WORDS)