Conformational analysis of SARS Covid using protein database
*C. Thurigha and S. Arul Mugilan
P.G. & Research Department of Physics, Kamarajar Government Arts College, Surandai-627859, Tamilnadu, (India), Affiliated to Manonmaniam Sundaranar University, Abishekapatti, Tirunelveli-627012, Tamilnadu, (India) *Register Number : 21211062132001 *e-mail: thuriakash@gmail.com
ABSTRACT
Globally, 10 million people have been infected by the COVID- 19-causing severe acute respiratory syndrome coronavirus 2 (SARSCoV- 2). Due to the coronavirus’s fast spread, its DNA has undergone significant changes. Biologists can considerably benefit from the secondary structure of a protein sequence in the creation and testing of hypotheses. Proteins are crucial for the proper operation of living things. Using bioinformatics databases, structural biologists may extrapolate secondary structural components from amino acid sequences. It has been demonstrated that the relationship between bond length and angle created with an adjacent bond in simple molecules is inverse, with shorter bond lengths resulting from bigger bond angles. Bond order is the whole variety of bonds between two atoms. When Bond Length is the measurement of the space between two atoms within a molecule. It is closely associated with stability. In this project, the conformational analysis of amino acids and sequential pair should be derived. With the use of Python and RasMol programming, calculations of SARS Covid Spike protein can be determined. α - helix, which makes up 30% of typical globular proteins, which are the most prevalent secondary structure. Various interactions (α helix & β sheet) of Protein folding result from unpaired interactions between α- helix and β- sheets. This research gives in-depth insights into the structure and dynamics of the SARS-CoV-2 protein that might be used to develop strong and specific inhibitors that target the membrane protein and are used in the process of creating drugs.