Structural and dynamics behavior of native endoglucanase from fusarium oxysporum

Molecular dynamics methods are very useful tool in understanding the behavior of the enzymes at higher temperatures. In this work we employ molecular dynamics simulation of an endoglucanase from Fusarium oxysporum to examine its structural and dynamics behavior at 80°C, by analyzing the root mean...

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Main Authors:	Ibrahim Ali , Noorbatcha, Waesoho, S., Hamzah, Mohd. Salleh
Format:	Article
Language:	English
Published:	INSI Publications 2012
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/17993/ http://irep.iium.edu.my/17993/ http://irep.iium.edu.my/17993/1/EGFO_AJBAS2012_Jan_89-92.pdf

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recordtype	eprints
spelling	iium-179932016-12-15T07:36:30Z http://irep.iium.edu.my/17993/ Structural and dynamics behavior of native endoglucanase from fusarium oxysporum Ibrahim Ali , Noorbatcha Waesoho, S. Hamzah, Mohd. Salleh TP248.13 Biotechnology Molecular dynamics methods are very useful tool in understanding the behavior of the enzymes at higher temperatures. In this work we employ molecular dynamics simulation of an endoglucanase from Fusarium oxysporum to examine its structural and dynamics behavior at 80°C, by analyzing the root mean square derivation (RMSD) from the initial structure. The RMSD values of coil and turn regions are found to be higher compared to helix and β-sheet regions. The surface area of the structure is found to have larger RMSD compared to the buried part of the enzyme, due the β-jelly roll nature of the enzyme. For the same reasons, the number of hydrogen bonds between among residues in β-sheet is found to larger compared to those in the coil regions. However, the number of hydrogen bonds between water and proteins is highest in turn regions and lowest in helix regions. The turn regions connecting the 310-helix are found to fluctuate more rapidly compared to the other parts of the enzyme. These factors can explain the loss of the activity of the enzyme at high temperatures. Key word: Endoglucanase, Molecular dynamics simulation, turn regions, Cel7B, hydrogen bonds. INSI Publications 2012-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/17993/1/EGFO_AJBAS2012_Jan_89-92.pdf Ibrahim Ali , Noorbatcha and Waesoho, S. and Hamzah, Mohd. Salleh (2012) Structural and dynamics behavior of native endoglucanase from fusarium oxysporum. Australian Journal of Basic and Applied Sciences, 6 (1). pp. 89-92. ISSN 1991-8178 http://www.insipub.com/index.html
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Ibrahim Ali , Noorbatcha Waesoho, S. Hamzah, Mohd. Salleh Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
description	Molecular dynamics methods are very useful tool in understanding the behavior of the enzymes at higher temperatures. In this work we employ molecular dynamics simulation of an endoglucanase from Fusarium oxysporum to examine its structural and dynamics behavior at 80°C, by analyzing the root mean square derivation (RMSD) from the initial structure. The RMSD values of coil and turn regions are found to be higher compared to helix and β-sheet regions. The surface area of the structure is found to have larger RMSD compared to the buried part of the enzyme, due the β-jelly roll nature of the enzyme. For the same reasons, the number of hydrogen bonds between among residues in β-sheet is found to larger compared to those in the coil regions. However, the number of hydrogen bonds between water and proteins is highest in turn regions and lowest in helix regions. The turn regions connecting the 310-helix are found to fluctuate more rapidly compared to the other parts of the enzyme. These factors can explain the loss of the activity of the enzyme at high temperatures. Key word: Endoglucanase, Molecular dynamics simulation, turn regions, Cel7B, hydrogen bonds.
format	Article
author	Ibrahim Ali , Noorbatcha Waesoho, S. Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali , Noorbatcha Waesoho, S. Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali , Noorbatcha
title	Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
title_short	Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
title_full	Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
title_fullStr	Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
title_full_unstemmed	Structural and dynamics behavior of native endoglucanase from fusarium oxysporum
title_sort	structural and dynamics behavior of native endoglucanase from fusarium oxysporum
publisher	INSI Publications
publishDate	2012
url	http://irep.iium.edu.my/17993/ http://irep.iium.edu.my/17993/ http://irep.iium.edu.my/17993/1/EGFO_AJBAS2012_Jan_89-92.pdf
first_indexed	2023-09-18T20:27:02Z
last_indexed	2023-09-18T20:27:02Z
_version_	1777408485132075008

Structural and dynamics behavior of native endoglucanase from fusarium oxysporum

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