A new approach to the evaluation of protein secondary structure predictions at the level of the elements of secondary structure.
For many purposes, such as the prediction of the class of protein folds, the existence of an element of secondary structure rather than its precise position and length must be defined correctly. However, most methods for the evaluation of secondary structure prediction consider success in terms of the percentage of individual amino acids predicted correctly. In this paper the success in predicting elements of secondary structure is discussed. The number of overlapping residues in the predicted and observed secondary structures were considered as a function of the total number of amino acids in the observed and predicted secondary structures. A matrix search procedure was used to remove the ambiguity which similar studies may have had in defining the equivalent secondary structures between predicted and observed structures. In this study a loop was treated in the same way as an alpha-helix and a beta-strand. To describe the accuracy at the level of elements of secondary structure, a set of parameters was defined, similar to those used commonly at the level of individual amino acids. This approach was used to assess the methods of Chou and Fasman (1974b, Biochemistry, 13, 222-245), Lim (1974b, J. Mol. Biol., 88, 873-894) and Garnier et al. (1978, J. Mol. Biol., 120, 97-120). It was found that these methods were much poorer at the secondary structure level than at the amino acid level. This approach can be used generally for secondary structure prediction methods.
Zhu
Z Y
ZY
Department of Crystallography, Birkbeck College, University of London, UK.
D000596:Amino Acids / Q000032:analysis; D016208:Databases, Factual; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D000596:Amino Acids; D011506:Proteins