In-Silico Analysis of Silk Serpin-2 Protein from Arachnocampa richardsae.

Publication Type:Journal Article
Year of Publication:2020
Authors:Chougale, A., Mantri, S., Kagale, S., Vedante S.
Journal:IJISET - International Journal of Innovative Science, Engineering & Technology

Silk Serpin-2 protein originates in Arachnocampa richardsae species which exhibits the presence of unexplored nucleotide sequence. Whole-genome annotations for Arachnocampa richardsae have not been accomplished and there are no known functions of Silk Serpin-2 until now. Therefore in this paper, we studied specifications like phylogenetic analysis, conservative residue, and conserved domain, secondary and 3D structure, physicochemical properties, and functional importance of Silk Serpin-2. The methodology used for the study involve software tools like MEGA X, Bio Edit, PSIPRED and Swissprot for the overall insilico study of the Silk Serpin-2 protein. Reliable and effective methods for 3D structure modeling were used and validated using the Ramachandran Plot. Results showed that the presence of silk Serpin-2 in the cell is responsible for many processes like regulation of metabolic process (88.08%), catabolic processes (69%), and catalytic activity (85.7%). The tools were used to discover the physicochemical properties from number of amino acids to the instability index. The secondary structure and 3D model of the protein were predicted which represented valid amino acid percentage in the allowed region of Ramachandran plot. The study may prove to be a reference for revealing further applications of the protein Silk Serpin-2 and the implementation of this technique will aid to expose other unknown proteins.

Taxonomy checked: 
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Thu, 2020-07-30 17:26 -- vblago
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