Structural Bioinformatics of Neisseria meningitidis Proteins - Rashid, Yasmeen
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Neisseria meningitidis genome contains 2158 protein coding regions. Nearly, half of the ORFs belongs to different functional classes. Sequence analysis of N. meningitidis hypothetical proteins using InterProScan and MPsrch resulted in the identification of 9 putative peptidases. Elegant bioinformatics studies provided functional information regarding the ORF NMB1147 to be an aspartate protease with a protein fold similar to CapA protein. Molecular cloning and expression of synthetic NMB1147 gene was carried out. The NMB1147 protein was expressed as inclusion bodies which were then solubilized…mehr

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Produktbeschreibung
Neisseria meningitidis genome contains 2158 protein coding regions. Nearly, half of the ORFs belongs to different functional classes. Sequence analysis of N. meningitidis hypothetical proteins using InterProScan and MPsrch resulted in the identification of 9 putative peptidases. Elegant bioinformatics studies provided functional information regarding the ORF NMB1147 to be an aspartate protease with a protein fold similar to CapA protein. Molecular cloning and expression of synthetic NMB1147 gene was carried out. The NMB1147 protein was expressed as inclusion bodies which were then solubilized followed by purification and refolding. Functional studies of HslVU protease-chaperone complex were also carried out for the identification of small molecules capable of activating HslV protease in the absence of its allosteric activator, HslU or HslU C-tail, using virtual screening of an in-house WADB compound library. Structural bioinformatics studies of four N. meningitidis proteins were also carried out.
Autorenporträt
Dr. Yasmeen Rashid d/o Waris Rashid is currently working as an assistant professor at Dow University of Health Sciences, Karachi, Pakistan. She graduated from Department of Biochemistry, University of Karachi and completed her Doctoral dissertation in 2011 from ICCBS, University of Karachi, Pakistan.