Support vector machines for the classification and prediction of β‐turn types
- 20 June 2002
- journal article
- research article
- Published by Wiley in Journal of Peptide Science
- Vol. 8 (7) , 297-301
- https://doi.org/10.1002/psc.401
Abstract
The support vector machines (SVMs) method is proposed because it can reflect the sequence‐coupling effect for a tetrapeptide in not only a β‐turn or non‐β‐turn, but also in different types of β‐turn. The results of the model for 6022 tetrapeptides indicate that the rates of self‐consistency for β‐turn types I, I′, II, II′, VI and VIII and non‐β‐turns are 99.92%, 96.8%, 98.02%, 97.75%, 100%, 97.19% and 100%, respectively. Using these training data, the rate of correct prediction by the SVMs for a given protein: rubredoxin (54 residues, 51 tetrapeptides) which includes 12 β‐turn type I tetrapeptides, 1 β‐turn type II tetrapeptide and 38 non‐β‐turns reached 82.4%. The high quality of prediction of the SVMs implies that the formation of different β‐turn types or non‐β‐turns is considerably correlated with the sequence of a tetrapeptide. The SVMs can save CPU time and avoid the overfitting problem compared with the neural network method. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.Keywords
This publication has 13 references indexed in Scilit:
- Turns in Peptides and ProteinsPublished by Elsevier ,2008
- Analysis and prediction of the different types of β-turn in proteinsPublished by Elsevier ,2004
- The Nature of Statistical Learning TheoryPublished by Springer Nature ,1995
- A revised set of potentials for β‐turn formation in proteinsProtein Science, 1994
- Prediction of β-turns in proteins using neural networksProtein Engineering, Design and Selection, 1989
- Turn prediction in proteins using a pattern-matching approachBiochemistry, 1986
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- Chain reversals in proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973