Cargando…

iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition

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 uncharacteri...

Descripción completa

Detalles Bibliográficos
Autores principales: Ehsan, Asma, Mahmood, Muhammad K., Khan, Yaser D., Barukab, Omar M., Khan, Sher A., Chou, Kuo-Chen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Science Publishers 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6728902/
https://www.ncbi.nlm.nih.gov/pubmed/31555063
http://dx.doi.org/10.2174/1389202920666190325162307
_version_ 1783449502371282944
author Ehsan, Asma
Mahmood, Muhammad K.
Khan, Yaser D.
Barukab, Omar M.
Khan, Sher A.
Chou, Kuo-Chen
author_facet Ehsan, Asma
Mahmood, Muhammad K.
Khan, Yaser D.
Barukab, Omar M.
Khan, Sher A.
Chou, Kuo-Chen
author_sort Ehsan, Asma
collection PubMed
description 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.
format Online
Article
Text
id pubmed-6728902
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Bentham Science Publishers
record_format MEDLINE/PubMed
spelling pubmed-67289022019-09-25 iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition Ehsan, Asma Mahmood, Muhammad K. Khan, Yaser D. Barukab, Omar M. Khan, Sher A. Chou, Kuo-Chen Curr Genomics Article 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. Bentham Science Publishers 2019-02 2019-02 /pmc/articles/PMC6728902/ /pubmed/31555063 http://dx.doi.org/10.2174/1389202920666190325162307 Text en © 2019 Bentham Science Publishers https://creativecommons.org/licenses/by-nc/4.0/legalcode This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Ehsan, Asma
Mahmood, Muhammad K.
Khan, Yaser D.
Barukab, Omar M.
Khan, Sher A.
Chou, Kuo-Chen
iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title_full iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title_fullStr iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title_full_unstemmed iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title_short iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature via Chou's 5-Step Rule and General Pseudo Amino Acid Composition
title_sort ihyd-pseaac (epsv): identifying hydroxylation sites in proteins by extracting enhanced position and sequence variant feature via chou's 5-step rule and general pseudo amino acid composition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6728902/
https://www.ncbi.nlm.nih.gov/pubmed/31555063
http://dx.doi.org/10.2174/1389202920666190325162307
work_keys_str_mv AT ehsanasma ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition
AT mahmoodmuhammadk ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition
AT khanyaserd ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition
AT barukabomarm ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition
AT khanshera ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition
AT choukuochen ihydpseaacepsvidentifyinghydroxylationsitesinproteinsbyextractingenhancedpositionandsequencevariantfeatureviachous5stepruleandgeneralpseudoaminoacidcomposition