Please use this identifier to cite or link to this item: https://hdl.handle.net/10321/1786
DC FieldValueLanguage
dc.contributor.authorKhan, Faez Iqbal-
dc.contributor.authorGovender, Algasan-
dc.contributor.authorPermaul, Kugen-
dc.contributor.authorSingh, Suren-
dc.contributor.authorBisetty, Krishna-
dc.date.accessioned2017-01-30T10:40:01Z-
dc.date.available2017-01-30T10:40:01Z-
dc.date.issued2015-
dc.identifier.citationKhan, F. I. et al. Thermostable chitinase II from Thermomyces lanuginosus SSBP: Cloning, structure prediction and molecular dynamics simulations. Journal of Theoretical Biology. 374: 107-114.en_US
dc.identifier.issn0022-5193 (print)-
dc.identifier.issn1095-8541 (online)-
dc.identifier.urihttp://hdl.handle.net/10321/1786-
dc.description.abstractThermomyces lanuginosus is a thermophilic fungus that produces large number of industrially-significant enzymes owing to their inherent stability at high temperatures and wide range of pH optima, including thermostable chitinases that have not been fully characterized. Here, we report cloning, characterization and structure prediction of a gene encoding thermostable chitinase II. Sequence analysis revealed that chitinase II gene encodes a 343 amino acid protein of molecular weight 36.65 kDa. Our study reports thatchitinase II exhibits a well-defined TIM-barrel topology with an eight-stranded α/β domain. Structural analysis and molecular docking studies suggested that Glu176 is essential for enzyme activity. Folding studies of chitinase II using molecular dynamics simulations clearly demonstrated that the stability of the protein was evenly distributed at 350 K.en_US
dc.format.extent8 pen_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofJournal of theoretical biology (Online)-
dc.subjectChitinen_US
dc.subjectTIM-barrelen_US
dc.subjectMD simulationsen_US
dc.subjectStabilityen_US
dc.subjectMolecular dockingen_US
dc.titleThermostable chitinase II from Thermomyces lanuginosus SSBP: Cloning, structure prediction and molecular dynamics simulationsen_US
dc.typeArticleen_US
dc.publisher.urihttp://dx.doi.org/10.1016/j.jtbi.2015.03.035en_US
dc.dut-rims.pubnumDUT-005135en_US
dc.description.availabilityCopyright: 2015. Elsevier. 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 Theoretical Biology, Vol 374, 107-114en_US
local.sdgSDG05-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.fulltextNo Fulltext-
Appears in Collections:Research Publications (Applied Sciences)
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