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Updated: Jan 19, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant
Asma Ehsan1, Muhammad K Mahmood1, Yaser D Khan1
11Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Background:
In various biological processes and cell functions, Post Translational Modifications (PTMs) bear critical significance. Hydroxylation of proline residue is one kind of PTM, which occurs following protein synthesis. The experimental determination of hydroxyproline sites in an uncharacterized protein sequence requires extensive, time-consuming and expensive tests.
Methods:
With the torrential slide of protein sequences produced in the post-genomic age, certain remarkable computational strategies are desired to overwhelm the issue. Keeping in view the composition and sequence order effect within polypeptide chains, an innovative in-silico> predictor via a mathematical model is proposed.
Results:
Later, it was stringently verified using self-consistency, cross-validation and jackknife tests on benchmark datasets. It was established after a rigorous jackknife test that the new predictor values are superior to the values predicted by previous methodologies.
Conclusion:
This new mathematical technique is the most appropriate and encouraging as compared with the existing models.
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