SARS-CoV-2 Spike Protein Reseptör Bağlanma Bölgesinde L18F Mutasyonunun Homoloji Modellemesi

Proteins have unique properties to participate in many structural and physiological processes. Knowledge of the three-dimensional structure proteins is important understand their roles processes functions these Any defect due mutations can cause diseases, treatment unresponsiveness, drug resistance development. The recent emergence new SARS-CoV-2 variants containing that accelerate spread virus by affecting infectiousness has been concern. In study, visualization homology model investigation chemical L18F mutation responsible for formation mutant type spike protein via silico approach was intended. this amino acid number, molecular weight, theoretical pI value, percentage composition acids, total negatively charged residue positively atomic composition, formula, molar extinction coefficient, aliphatic index, average hydropathy were calculated ProtParam. FASTA sequence used models UCSF Chimera wild-type mutant-type proteins. Basic calculations also displayed on BIOVIA Discovery Studio Visualizer. ΔΔG value changes stability predicted I-Mutant Suite software. We detected location near a highly conserved position may not damage.