WoS İndeksli Yayınlar Koleksiyonu
Permanent URI for this collectionhttps://hdl.handle.net/20.500.12573/394
Browse
3 results
Search Results
Conference Object Citation - WoS: 3Citation - Scopus: 3Template Scoring Methods for Protein Torsion Angle Prediction(Springer-Verlag Berlin, 2015) Aydin, Zafer; Baker, David; Noble, William StaffordPrediction of backbone torsion angles provides important constraints about the 3D structure of a protein and is receiving a growing interest in the structure prediction community. In this paper, we introduce a three-stage machine learning classifier to predict the 7-state torsion angles of a protein. The first two stages employ dynamic Bayesian and neural networks to produce an ab-initio prediction of torsion angle states starting from sequence profiles. The third stage is a committee classifier, which combines the ab-initio prediction with a structural frequency profile derived from templates obtained by HHsearch. We develop several structural profile models and obtain significant improvements over the Laplacian scoring technique through: (1) scaling templates by integer powers of sequence identity score, (2) incorporating other alignment scores as multiplicative factors (3) adjusting or optimizing parameters of the profile models with respect to the similarity interval of the target. We also demonstrate that the torsion angle prediction accuracy improves at all levels of target-template similarity even when templates are distant from the target. The improvement is at significantly higher rates as template structures gradually get closer to target.Article Citation - WoS: 2Citation - Scopus: 2Structural Profile Matrices for Predicting Structural Properties of Proteins(World Scientific Publ Co Pte Ltd, 2020-07-10) Azginoglu, Nuh; Aydin, Zafer; Celik, MetePredicting structural properties of proteins plays a key role in predicting the 3D structure of proteins. In this study, new structural profile matrices (SPM) are developed for protein secondary structure, solvent accessibility and torsion angle class predictions, which could be used as input to 3D prediction algorithms. The structural templates employed in computing SPMs are detected by eight alignment methods in LOMETS server, gap affine alignment method, ScanProsite, PfamScan, and HHblits. The contribution of each template is weighted by its similarity to target, which is assessed by several sequence alignment scores. For comparison, the SPMs are also computed using Homolpro, which uses BLAST for target template alignments and does not assign weights to templates. Incorporating the SPMs into DSPRED classifier, the prediction accuracy improves significantly as demonstrated by cross-validation experiments on two difficult benchmarks. The most accurate predictions are obtained using the SPMs derived by threading methods in LOMETS server. On the other hand, the computational cost of computing these SPMs was the highest.Article Citation - WoS: 6Citation - Scopus: 8Dimensionality Reduction for Protein Secondary Structure and Solvent Accesibility Prediction(World Scientific Publ Co Pte Ltd, 2018-10) Aydin, Zafer; Kaynar, Oguz; Gormez, YasinSecondary structure and solvent accessibility prediction provide valuable information for estimating the three dimensional structure of a protein. As new feature extraction methods are developed the dimensionality of the input feature space increases steadily. Reducing the number of dimensions provides several advantages such as faster model training, faster prediction and noise elimination. In this work, several dimensionality reduction techniques have been employed including various feature selection methods, autoencoders and PCA for protein secondary structure and solvent accessibility prediction. The reduced feature set is used to train a support vector machine at the second stage of a hybrid classifier. Cross-validation experiments on two difficult benchmarks demonstrate that the dimension of the input space can be reduced substantially while maintaining the prediction accuracy. This will enable the incorporation of additional informative features derived for predicting the structural properties of proteins without reducing the accuracy due to overfitting.