Chee Fah Wong1, Raja Noor Zaliha Raja Abd. Rahman, Mahiran Basri and Abu Bakar Salleh
Accepted Abstracts: Drug Design
The principle of structure homology modeling is to gain better understanding of functions and inter/intramolecular interactions of proteins in aqueous and non-aqueous environments. This study was focused on elucidation of three dimensional structure of the mature elastase strain K using 3 homology modeling softwares; Discovery StudioŽ, 3D Jigsaw and Swiss Model. The predicted structure of the protein, as resulted from multiple stages and steps of energy minimization and validation, had led to the discovery of several intramolecular disulphide bridges which deemed essential for the protein stability in organic solvents especially methanol. Clear correlations were established between concentrations of methanol and changes in secondary structures of elastase strain K as its activity enhancement and stability were explained by just the slight change of α-helical structures, presumably preserving the catalytic triad in active site at the α-helical region (as predicted from homology modeling). In contrast, sudden decrease of the protein stability in higher methanol concentrations was described by the total ruptures of the helical structures, and thus resulted in the increase of random coil.
Dr. Wong Chee Fah is a senior lecturer in microbiology. His doctoral studies had highlighted several achievements and novelties including construction of vectors which had led to the understanding of plasmid-host relationship, the protein overexpression by constructed vectors, protein dimerization and most importantly, the behavior of enzymes in organic solvents. He has contributed to several ISI-cited journals besides numerous abstracts and proceedings. He has a pending patent of constructed shuttle vectors and purified enzyme as well as the remarkable stability of the enzyme in organic solvents.