Comparison of amino acid occurrence and composition for predicting protein folds
| dc.creator | Taguchi, Y-h. | |
| dc.creator | Gromiha, M. Michael | |
| dc.date | 2006-09-25 | |
| dc.date | 2007-05-10 | |
| dc.date.accessioned | 2026-07-07T08:00:33Z | |
| dc.date.available | 2026-07-07T08:00:33Z | |
| dc.description | Background:Prediction of protein three-dimensional structures from amino acid sequences is a long-standing goal in computational/molecular biology. The successful discrimination of protein folds would help to improve the accuracy of protein 3D structure prediction. Results: In this work, we propose a method based on linear discriminant analysis (LDA) for recognizing proteins belonging to 30 different folds using the occurrence of amino acid residues in a set of 1612 proteins. The present method could discriminate the globular proteins from 30 major folding types with the sensitivity of 37%, which is comparable to or better than other methods in the literature. A web server has been developed for predicting the folding type of the protein from amino acid sequence and it is available at http://granular.com/PROLDA/. Conclusions:Linear discriminant analysis based on amino acid occurrence could successfully recognize protein folds. The present method has several advantages such as, (i) it directly predicts the folding type of a protein without performing pair-wise comparisons, (ii) it can discriminate folds among large number of proteins and (iii) it is very fast to obtain the results. This is a simple method, which can be easily incorporated in any other structure prediction algorithms. | |
| dc.identifier | https://arxiv.org/abs/q-bio/0609037 | |
| dc.identifier | http://arxiv.org/abs/q-bio/0609037 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/128689 | |
| dc.subject | Biomolecules | |
| dc.subject | Soft Condensed Matter | |
| dc.subject | Adaptation and Self-Organizing Systems | |
| dc.subject | Quantitative Methods | |
| dc.title | Comparison of amino acid occurrence and composition for predicting protein folds | |
| dc.type | text |