Mutations in the SARS CoV-2 spike protein may cause functional changes in the protein quaternary structure

Abstract Objectives This study aimed to model the changes resulting from mutations in surface (spike/S) glycoproteins, which play a key role entry of severe acute respiratory syndrome coronavirus-2 (SARS CoV-2) into host cells, protein quaternary structure and evaluate their possible effects on functional structure. Methods Genome sequence information SARS CoV-2-infected patients located Turkey was obtained GISAID EpiCoV database. Structural analysis spike proteins done using bioinformatics tools (MAFFT, PSIPRED, ProMod3, PyMoL DynOmics). Results We identified 76 Thr>Ile N -terminal domain; 468 Ile>Val receptor binding site 614 Asp>Gly, 679 Asn>Lys, 771 Ala>Val 772 Val>Ile S1 subunit. It has been observed that mutations, except those residues 772, may cause significant conformational, topological electrostatic determined transform formation can mask affect affinity. Conclusions considered CoV-2 S glycoprotein severity disease.