Protein Sequence Analysis of Newcastle (Paramyxovirus) in Poultry

Abstract: A total of ten (10) Newcastle proteins of poultry were retrieved from the GenBank (www.ncbi.nlm. nih.gov). The Genbank accession numbers of the sequences and sequence variations were used to investigate the molecular identity of various newcastle proteins. The phyco-chemical properties of newcastle proteins were performed using protparam tool. The isoelectric point (pI), extinction coefficient (EC); instability index (II), aliphatic index (AI) and grand average of hydropathicity (GRAVY) were also computed. The study reveals that 90% and 10% of the pI of Newcastle protein were basic nature and acidic in nature respectively. The EC and II of Newcastle protein shows better stability which is an indication of resistance to mutation. AI for all the protein is <100. This indicates that the newcastle protein are not thermally stable. The GRAVY, 90% of the protein were negative and only 10% were positive. The positive values indicate solubility in water while negative is not soluble in water. The amino acid composition of newcastle proteins indicate that they are rich in serine and asparagines which are hydroxyl amino acid which is non reactive and can play a role in substrate recognition which mean they are resistant to mutation. The prediction of secondary structure was performed using SOPMA. The proteins are more of random coil structure then followed by alpha helix which shows that they are not thermally stable. Phyre2 server was used to predict the 3D structure of newcastle proteins. Study on pharmacogenetic and mutagenesis is needed regarding this finding. Keywords: Protein, Newcastle and Sequence. Title: Protein Sequence Analysis of Newcastle (Paramyxovirus) in Poultry Author: Ayuba. Dauda, Haruna Duwa, Jummai Adamu Yaska, Joseph Ochoche Egahi, Yarima Shettima Kollo International Journal of Interdisciplinary Research and Innovations ISSN 2348-1218 (print), ISSN 2348-1226 (online) Research Publish Journals

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