OH-PRED: prediction of protein hydroxylation sites by incorporating adapted normal distribution bi-profile Bayes feature extraction and physicochemical properties of amino acids. Issue 4 (12th March 2017)
- Record Type:
- Journal Article
- Title:
- OH-PRED: prediction of protein hydroxylation sites by incorporating adapted normal distribution bi-profile Bayes feature extraction and physicochemical properties of amino acids. Issue 4 (12th March 2017)
- Main Title:
- OH-PRED: prediction of protein hydroxylation sites by incorporating adapted normal distribution bi-profile Bayes feature extraction and physicochemical properties of amino acids
- Authors:
- Jia, Cang-Zhi
He, Wen-Ying
Yao, Yu-Hua - Abstract:
- Abstract : Hydroxylation of proline or lysine residues in proteins is a common post-translational modification event, and such modifications are found in many physiological and pathological processes. Nonetheless, the exact molecular mechanism of hydroxylation remains under investigation. Because experimental identification of hydroxylation is time-consuming and expensive, bioinformatics tools with high accuracy represent desirable alternatives for large-scale rapid identification of protein hydroxylation sites. In view of this, we developed a supporter vector machine-based tool, OH-PRED, for the prediction of protein hydroxylation sites using the adapted normal distribution bi-profile Bayes feature extraction in combination with the physicochemical property indexes of the amino acids. In a jackknife cross validation, OH-PRED yields an accuracy of 91.88% and a Matthew's correlation coefficient (MCC) of 0.838 for the prediction of hydroxyproline sites, and yields an accuracy of 97.42% and a MCC of 0.949 for the prediction of hydroxylysine sites. These results demonstrate that OH-PRED increased significantly the prediction accuracy of hydroxyproline and hydroxylysine sites by 7.37 and 14.09%, respectively, when compared with the latest predictor PredHydroxy. In independent tests, OH-PRED also outperforms previously published methods.
- Is Part Of:
- Journal of biomolecular structure & dynamics. Volume 35:Issue 4(2017)
- Journal:
- Journal of biomolecular structure & dynamics
- Issue:
- Volume 35:Issue 4(2017)
- Issue Display:
- Volume 35, Issue 4 (2017)
- Year:
- 2017
- Volume:
- 35
- Issue:
- 4
- Issue Sort Value:
- 2017-0035-0004-0000
- Page Start:
- 829
- Page End:
- 835
- Publication Date:
- 2017-03-12
- Subjects:
- protein hydroxylation -- physicochemical properties -- ANBPB -- SVM
Biomolecules -- Periodicals
Molecular structure -- Periodicals
Molecular Biology -- Periodicals
Biomechanics -- Periodicals
572 - Journal URLs:
- http://www.tandfonline.com/loi/tbsd20 ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/07391102.2016.1163294 ↗
- Languages:
- English
- ISSNs:
- 0739-1102
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4953.850000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 9903.xml