Effect of Ion Pair on thermostability of F1 protease: integration of computational and experimental approaches

Raja Noor Zaliha Raja Abd Rahman, and Noor Dina Muhd Noor, and Noor Azlina Ibrahim, and Abu Bakar Salleh, and Mahiran Basri, (2012) Effect of Ion Pair on thermostability of F1 protease: integration of computational and experimental approaches. Journal of Microbiology and Biotechnology, 22 (1). pp. 34-45. ISSN 1017-7825

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Abstract

A thermophilic Bacillus stearothermophilus F1 produces an extremely thermostable serine protease. The F1 protease sequence was used to predict its three-dimensional (3D) structure to provide better insights into the relationship between the protein structure and biological function and to identify opportunities for protein engineering. The final model was evaluated to ensure its accuracy using three independent methods: Procheck, Verify3D, and Errat. The predicted 3D structure of F1 protease was compared with the crystal structure of serine proteases from mesophilic bacteria and archaea, and led to the identification of features that were related to protein stabilization. Higher thermostability correlated with an increased number of residues that were involved in ion pairs or networks of ion pairs. Therefore, the mutants W200R and D58S were designed using site-directed mutagenesis to investigate F1 protease stability. The effects of addition and disruption of ion pair networks on the activity and various stabilities of mutant F1 proteases were compared with those of the wild-type F1 protease.

Item Type: Non-Indexed Article
Keywords: Site-directed mutagenesis - Thermostability - Ion pairs
Faculty: Faculty of Agro - Based Industry
Deposited By: Dr Noor Azlina Ibrahim
Date Deposited: 24 Jun 2013 08:06
Last Modified: 24 Jun 2013 08:06
URI: http://umkeprints.umk.edu.my/id/eprint/1665

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