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  • Article: In silico Modelling and Analysis of Aquaporin Protein Sequences of the Catfish Heteropneustes fossilis (JCB-2013-0037)
    Tazmeen Shirazi, Abhigyan Nath, Dr. Radha Chaube
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    ABSTRACT: ABSTRACT Aquaporins (AQPs) are membrane channel proteins which facilitate the rapid transport of water across cellular membrane and are of fundamental importance to the control of cell volume and transcellular water traffic. In the present study, using bioinformatics tools in silico modelling and analysis of aquaporin protein sequences of catfish Heteropneustes fossilis was conducted. The catfish H. fossilis Aqp1b cDNA encodes a 263 amino acid length sequence. The in silico analysis of sequence found single domain of cd00333 :MIP which is Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. A model has been built with the predicted peptide sequence of Aqp1b of catfish oocyte that include the six potential transmembrane domain and two Asn-Pro-Ala (NPA) motifs. Further, various tools helped us in identification of phosphorylation sites, structure modelling and comparison of structure with higher and lower vertebrates. The present study suggests that this ovarian catfish peptide has got unique evolutionary significance by having close resemblance to human aquaporin in structural homology.
    Journal of Computational Biology 03/2013; · 1.55 Impact Factor

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