Özet:

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

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