HOMOLOGY MODELING AND INSILICO ANALYSIS OF PROTEINS OF BOMBYX MORI - “A GREEN APPROACH”
Aashika A., Rubalakshmi G.*, Nirubama K. and Prabhakaran S.
ABSTRACT
Sericin is a natural polymer produced by Silkworm also known as Bombyx mori. The Silk worm wounds around itself a fiber, cocoon which keeps together two fibroin filaments. The fibrion forms central core and sericin forms envelop and is water soluble. In this present study, 10 proteins of Sericin were analysed using bioinformatics tools. Structural prediction and functional characterization of proteins of Sericin were done using Expasy Protparam server, 3D structure was done using SWISS MODEL. Plants of different family showing identity 30% and above were selected and its sequences retrieved, aligned using Clustal Omega. Phylogenetic tree was constructed for the aligned sequence. Structure prediction showed that α – helix, random coil, β – turn and extended strand predominates. Transmembrane region was found in NADPH cytochrome P450 reductase, cytochrome c oxidase subunit 1, nicotonic acetylcholine receptor proteins. NADPH cytochrome P450 reductase possesses the abilty to reduce metals and hence Sericin was predicted for its ability to synthesis nanoparticles. Phylogenetic analysis of NADPH cytochrome P450 reductase of sericin reveals that the Bombycidae families are closely related. Thus, sericin is a potential biocompatible material for its biomedical applications.
Keywords: Bombyx mori, NADPH cytochrome P450 reductase, sericin, Phylogenetic analysis.
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