Bioinformatics Study on Structural Protein of Severe Acute Respiratory Syndrome Coronavirus 2 (Sars-Cov-2) For Better Understanding the Vaccine Development

Sumaira Gulzar; Saqib Hussain

The physical parameters shows that Surface protein contain highest amino acids, negatively charged residues, positively charged residues, EC and molecular weight than other proteins. The chemical factors show in proteins phenyl alanine and serine is totally absent in all structural proteins, there is a lack of histidine and glutamic acid in the protein envelope and a lack of cysteine in the nucleocapside phosphoprotein. The envelope, surface and membrane glycoprotein is rich in Leucine so have more affinity to the host cell receptor surface as stated in Luo et al, 1999 . Although glycine is more in nucleocapside phosphoprotein, researchers should be able to isolate the protein with little effort along with these data and iso-electric point value. Higher molecular weight of the surface glycoprotein suggests that its tertiary structure may contain strong amino acid side chains.Instability index surface, membrance and envelop glycoprotein is stable and nucleocapsid phosphoprotein is highly unstable Leaving the surface Glycoprotaein and nucleocapsid phosphoprotein all other protein are hydrophobic in nature. The prediction of trans-membrane in all structural proteins except Nucleocapsid Phosphoprotein shows the virus ability to reach the host with ease. This fairly simple method may help us understand how antivirals and vaccines could be produced against it Furthermore, as a beginning for docking studies (small and large scale) we are now offering homology models, Diverse knowledge of the molecular biology of SARS COV_2 is required to . CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.21.053199 doi: bioRxiv preprint learn more.