<?xml version="1.0" encoding="utf-8"?>
<Journal>
<Journal-Info>
<name>International Journal of Pharma and Bio Sciences</name>
<website>ijpbs.net</website>
<email>editorijpbs@rediffmail.com (or) editorofijpbs@yahoo.com (or) prasmol@rediffmail.com</email>
</Journal-Info>
<article>
<article-id pub-id-type='other'>10.22376/ijpbs.2019.10.1.p1-12</article-id>
<issue_number>Volume 2 Issue 3</issue_number>
<issue_period>2011 (July - September)</issue_period>
<title>Homology Modelling Of Polyphenol Oxidase From Solanum Melongena: Sequence Analysis And Structural Validation Studies – In Silico. </title>
<abstract>Polyphenol oxidase (PPO) typically found in the chloroplasts of plants, is an enzyme that brings about browning in fruits and vegetables. This browning is a common phenomenon which leads to decreased market value and economic loss. In order to interpret the mechanism of process by which Polyphenol oxidases in Solanum melongena are making browning reaction, it is important to know its 3D structure. Homology modeling was done by Modeller and Geno3D with a template sequence of PPO of Vitis vinifera. The 3 D structure of the protein was evaluated and validated using PROCHECK and Verify_3D. The favored and unfavored regions of the amino acid residue were indicated by the Ramachandran plot. The results represented 224 numbers of hydrogen bonds, 15 helices, 11 strands and 50 numbers of turns. The modeled protein structure was subjected to  lessThan i greaterThan In silico lessThan /i greaterThan  analysis using various bioinformatics tools. The significance of our study focuses on the 3 D structure prediction of this enzyme and  lessThan i greaterThan In silico lessThan /i greaterThan  analysis of its secondary structure.</abstract>
<authors>Medhavi Mallick, Koel Mukherjee And Neetha A.Udayakumar</authors>
<keywords>Polyphenol oxidase (PPO), Browning, Homology modeling, Motif,  Domain.</keywords>
<pages>319-328</pages>
</article>
</Journal>
