Please use this identifier to cite or link to this item:
|Title:||Thermostable chitinase II from Thermomyces lanuginosus SSBP : Cloning, structure prediction and molecular dynamics simulations||Authors:||Khan, Faez Iqbal
|Keywords:||Chitin;TIM-barrel;MD simulations;Stability;Molecular docking||Issue Date:||8-Apr-2015||Publisher:||Elsevier||Source:||Khan, F. I. et al. 2015. Thermostable chitinase II from Thermomyces lanuginosus SSBP: Cloning, structure prediction and molecular dynamics simulations. Journal of Theoretical Biology, 374: 107-114.||Abstract:||Thermomyces 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 that chitinase 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.||URI:||http://hdl.handle.net/10321/1607||ISSN:||0022-5193|
|Appears in Collections:||Research Publications (Applied Sciences)|
Show full item record
checked on Oct 20, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.