Please use this identifier to cite or link to this item:
https://hdl.handle.net/10321/2943
DC Field | Value | Language |
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dc.contributor.author | Khan, Faez Iqbal | en_US |
dc.contributor.author | Bisetty, Krishna | en_US |
dc.contributor.author | Gu, Ke-Ren | en_US |
dc.contributor.author | Singh, Suren | en_US |
dc.contributor.author | Permaul, Kugen | en_US |
dc.contributor.author | Hassan, Md. Imtaiyaz | en_US |
dc.contributor.author | Wei, Dong-Qing | en_US |
dc.date.accessioned | 2018-03-26T07:59:23Z | - |
dc.date.available | 2018-03-26T07:59:23Z | - |
dc.date.issued | 2016-09-22 | - |
dc.identifier.citation | Khan, 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: 10.1080/08927022.2016.1237024 | en_US |
dc.identifier.issn | 0892-7022 | - |
dc.identifier.issn | 1029-0435 | - |
dc.identifier.uri | http://hdl.handle.net/10321/2943 | - |
dc.description.abstract | The 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.extent | 10 p | en_US |
dc.language.iso | en | en_US |
dc.publisher | Taylor and Fancis Online | en_US |
dc.relation.ispartof | Molecular simulation (Online) | en_US |
dc.subject | Chitinase | en_US |
dc.subject | TIM-barrel | en_US |
dc.subject | Protein stability | en_US |
dc.subject | Molecular docking | en_US |
dc.subject | GROMAC S | en_US |
dc.subject | Molecular dynamics simulation | en_US |
dc.title | Molecular dynamics simulation of chitinase I from Thermomyces lanuginosus SSBP to ensure optimal activity | en_US |
dc.type | Article | en_US |
dc.publisher.uri | https://www.tandfonline.com/doi/pdf/10.1080/08927022.2016.1237024?needAccess=true | en_US |
dc.dut-rims.pubnum | DUT-005779 | en_US |
dc.description.availability | Copyright: 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/10.1080/08927022.2016.1237024 | en_US |
dc.identifier.doi | 10.1080/08927022.2016.1237024 | - |
local.sdg | SDG05 | - |
item.openairetype | Article | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
Appears in Collections: | Research Publications (Applied Sciences) |
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