Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
Abstract Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to det...
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iium-301442014-01-13T00:55:07Z http://irep.iium.edu.my/30144/ Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Mohd. Salleh, Hamzah Amid, Azura TP248.13 Biotechnology Abstract Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to determine thermostability factors. The results suggest that, among secondary structure elements, loops have the most impact on the thermal stability of A. niger phytase. In addition, the location rather than the number of hydrogen bonds is found to have an important contribution to thermostability. The results also show that salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly. Springer 2013-05-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/30144/1/PhyA_Phytase_PJ_%282013%29_32-309-316.pdf Noorbatcha, Ibrahim Ali and Sultan, Anas Mufid Nasri and Mohd. Salleh, Hamzah and Amid, Azura (2013) Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study. Protein Journal, 32. pp. 309-316. ISSN 1572-3887 http://link.springer.com/article/10.1007%2Fs10930-013-9489-y 10.1007/s10930-013-9489-y |
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TP248.13 Biotechnology |
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TP248.13 Biotechnology Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Mohd. Salleh, Hamzah Amid, Azura Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
description |
Abstract Molecular dynamics simulation was used to
study the dynamic differences between native Aspergillus
niger PhyA phytase and a mutant with 20 % greater thermostability.
Atomic root mean square deviation, radius of
gyration, and number of hydrogen bonds and salt bridges
are examined to determine thermostability factors. The
results suggest that, among secondary structure elements,
loops have the most impact on the thermal stability of
A. niger phytase. In addition, the location rather than the
number of hydrogen bonds is found to have an important
contribution to thermostability. The results also show that
salt bridges may have stabilizing or destabilizing effect on
the enzyme and influence its thermostability accordingly. |
format |
Article |
author |
Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Mohd. Salleh, Hamzah Amid, Azura |
author_facet |
Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Mohd. Salleh, Hamzah Amid, Azura |
author_sort |
Noorbatcha, Ibrahim Ali |
title |
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
title_short |
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
title_full |
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
title_fullStr |
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
title_full_unstemmed |
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study |
title_sort |
understanding thermostability factors of aspergillus niger phya phytase: a molecular dynamics study |
publisher |
Springer |
publishDate |
2013 |
url |
http://irep.iium.edu.my/30144/ http://irep.iium.edu.my/30144/ http://irep.iium.edu.my/30144/ http://irep.iium.edu.my/30144/1/PhyA_Phytase_PJ_%282013%29_32-309-316.pdf |
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2023-09-18T20:44:15Z |
last_indexed |
2023-09-18T20:44:15Z |
_version_ |
1777409568326811648 |