Please use this identifier to cite or link to this item: http://hdl.handle.net/10321/2943
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dc.contributor.authorKhan, Faez Iqbal-
dc.contributor.authorBisetty, Krishna-
dc.contributor.authorGu, Ke-Ren-
dc.contributor.authorSingh, Suren-
dc.contributor.authorPermaul, Kugen-
dc.contributor.authorHassan, Md. Imtaiyaz-
dc.contributor.authorWei, Dong-Qing-
dc.date.accessioned2018-03-26T07:59:23Z-
dc.date.available2018-03-26T07:59:23Z-
dc.date.issued2016-09-22-
dc.identifier.citationKhan, F.I. et al. 2016. Molecular dynamics simulation of chitinase I from Thermomyces lanuginosus SSBP to ensure optimal activity. Molecular Simulation. 43(7): 480-490. DOI: 10.1080/08927022.2016.1237024en_US
dc.identifier.issn0892-7022-
dc.identifier.issn1029-0435-
dc.identifier.urihttp://hdl.handle.net/10321/2943-
dc.description.abstractThe fungal chitinase I obtained from Thermomyces lanuginosus SSBP, a thermophilic deuteromycete, has an optimum growth temperature and pH of 323.15 K and 6.5, respectively. This enzyme plays an important task in the defence mechanism of organisms against chitin-containing parasites by hydrolysing β-1, 4-linkages in chitin. It acts as both anti-fungal and biofouling agents, with some being thermostable and suitable for the industrial applications. Three-dimensional model of chitinase I enzyme was predicted and analysed using various bioinformatics tools. The structure of chitinase I exhibited a well-defined TIM barrel topology with an eight-stranded α/β domain. Structural analysis and folding studies at temperatures ranging from 300 to 375 K using 10 ns molecular dynamics simulations clearly showed the stability of the protein was evenly distributed even at higher temperatures, in accordance with the experimental results. We also carried out a number of 20 ns constant pH molecular dynamics simulations of chitinase I at a pH range 2–6 in a solvent. This work was aimed at establishing the optimum activity and stability profiles of chitinase I. We observed a strong conformational pH dependence of chitinase I and the enzyme retained their characteristic TIM barrel topology at low pH.en_US
dc.format.extent10 pen_US
dc.language.isoenen_US
dc.publisherTaylor and Fancis Onlineen_US
dc.subjectChitinaseen_US
dc.subjectTIM-barrelen_US
dc.subjectProtein stabilityen_US
dc.subjectMolecular dockingen_US
dc.subjectGROMAC Sen_US
dc.subjectMolecular dynamics simulationen_US
dc.titleMolecular dynamics simulation of chitinase I from Thermomyces lanuginosus SSBP to ensure optimal activityen_US
dc.typeArticleen_US
dc.publisher.urihttps://www.tandfonline.com/doi/pdf/10.1080/08927022.2016.1237024?needAccess=trueen_US
dc.dut-rims.pubnumDUT-005779en_US
dc.description.availabilityCopyright: 2016. Taylor & Francis Online. Due to copyright restrictions, only the abstract is available. For access to the full text item, please consult the publisher's website. The definitive version of the work is published in Journal of Molecular Simulation, Vol 43. Pages 480-490. https://doi.org/10.1080/08927022.2016.1237024en_US
item.fulltextNo Fulltext-
item.grantfulltextnone-
Appears in Collections:Research Publications (Applied Sciences)
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