Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies

Structural and dynamic factors responsible for the themostability of β-glucuronidase (GUS) are analyzed by performing molecular dynamics simulations of human, E. coli, T. maritima and mutated E. coli GUS at 300 K and 353 K. 3D structures of mesophilic and thermophilic GUS enzymes have been construc...

Full description

Bibliographic Details
Main Authors:	Ibrahim Ali , Noorbatcha, Hamzah, Mohd. Salleh
Format:	Conference or Workshop Item
Language:	English
Published:	2012
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/25988/ http://irep.iium.edu.my/25988/1/IBS2012_GUS_poster.pdf

id	iium-25988
recordtype	eprints
spelling	iium-259882013-01-02T06:24:14Z http://irep.iium.edu.my/25988/ Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh TP248.13 Biotechnology Structural and dynamic factors responsible for the themostability of β-glucuronidase (GUS) are analyzed by performing molecular dynamics simulations of human, E. coli, T. maritima and mutated E. coli GUS at 300 K and 353 K. 3D structures of mesophilic and thermophilic GUS enzymes have been constructed using homology modeling, based on the known crystal structure of human GUS enzyme. The flexibility of backbone atoms and amino acid residues, structural compactness, hydrogen bonds and salt bridges are analyzed during the simulation. The ability of the GUS enzymes to maintain their structural compactness and, similar backbone and residue fluctuations at a range of temperatures is found to be crucial in determining the thermostability. The presence of a large number of Glu-Arg salt bridge pairs stabilizes the structures of T. maritima GUS and mutant E. coli GUS at higher temperatures. The thermolabile residues 150-155 were found to have smaller fluctuations in mutated E. coli GUS. Keywords: human, E. coli, T. maritima and mutated E. coli β-glucuronidases (GUS); thermostability; molecular dynamics. 2012 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/25988/1/IBS2012_GUS_poster.pdf Ibrahim Ali , Noorbatcha and Hamzah, Mohd. Salleh (2012) Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies. In: International Biotechnology Symposium and Exhibition (IBS 2012), 16-21 September 2012, Daegu, Korea. (Unpublished)
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 Hamzah, Mohd. Salleh Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
description	Structural and dynamic factors responsible for the themostability of β-glucuronidase (GUS) are analyzed by performing molecular dynamics simulations of human, E. coli, T. maritima and mutated E. coli GUS at 300 K and 353 K. 3D structures of mesophilic and thermophilic GUS enzymes have been constructed using homology modeling, based on the known crystal structure of human GUS enzyme. The flexibility of backbone atoms and amino acid residues, structural compactness, hydrogen bonds and salt bridges are analyzed during the simulation. The ability of the GUS enzymes to maintain their structural compactness and, similar backbone and residue fluctuations at a range of temperatures is found to be crucial in determining the thermostability. The presence of a large number of Glu-Arg salt bridge pairs stabilizes the structures of T. maritima GUS and mutant E. coli GUS at higher temperatures. The thermolabile residues 150-155 were found to have smaller fluctuations in mutated E. coli GUS. Keywords: human, E. coli, T. maritima and mutated E. coli β-glucuronidases (GUS); thermostability; molecular dynamics.
format	Conference or Workshop Item
author	Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali , Noorbatcha
title	Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
title_short	Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
title_full	Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
title_fullStr	Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
title_full_unstemmed	Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies
title_sort	insights into thermostability of β-glucuronidase (gus) through molecular dynamics studies
publishDate	2012
url	http://irep.iium.edu.my/25988/ http://irep.iium.edu.my/25988/1/IBS2012_GUS_poster.pdf
first_indexed	2023-09-18T20:38:45Z
last_indexed	2023-09-18T20:38:45Z
_version_	1777409222823116800

Insights into Thermostability of β-glucuronidase (GUS) through molecular dynamics studies

Similar Items