title: On the relation between the predicted secondary structure and the protein size.
abstract: Accurately predicted protein secondary structure provides useful information for target selection, to analyze protein function and to predict higher dimensional structure. Existing research shows that more data + refined search = better prediction. We analyze relation between the prediction accuracy and another crucial factor, the protein size. Empirical tests performed with two secondary structure predictors on a large set of high-resolution, non-redundant proteins show that the average accuracies for small proteins (<100 residues) equal 73% and 54% for alpha-helices and beta-strands, respectively. The alpha-helix/beta-strand accuracies for very large proteins (>300 residues) equal 77%/68%, respectively. Similarly, the tests with three secondary structure content predictors show that the prediction errors for the small/very large proteins equal 0.13/0.09 and 0.09/0.06 for alpha-helix and beta-strand content, respectively. Our tests confirm that the secondary structure/content predictions for the very large proteins are characterized statistically significantly better quality than prediction for the small proteins. This is in contrast with the tertiary structure predictions in which higher accuracy is obtained for smaller proteins.
authors.affiliation: Department of Electrical and Computer Engineering, University of Alberta, 2nd floor, ECERF (9107 116 Street), Edmonton, AB, Canada T6G 2V4. lkurgan@ece.ualberta.ca
authors.forename: Lukasz
authors.initials: L
authors.lastname: Kurgan
mesh_terms: D000595:Amino Acid Sequence; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins