COVID-19 is increasingly affecting human health and global economy. Understanding the fundamental mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is highly demanded to develop treatments for COVID-19. SARS-CoV and SARS-CoV-2 share 92.06% identity in their N protein RBDs’ sequences, which results in very similar structures. However, the SARS-CoV-2 is more easily to spread. Utilizing multi-scale computational approaches, this work studied the fundamental mechanisms of the nucleocapsid (N) proteins of SARS-CoV and SARS-CoV-2, including their stabilities and binding strengths with RNAs at different pH values. Electrostatic potential on the surfaces of N proteins show that both the N proteins of SARS-CoV and SARS-CoV-2 have dominantly positive potential to attract RNAs. The binding forces between SARS-CoV N protein and RNAs at different distances are similar to that of SARS-CoV-2, both in directions and magnitudes. The electric filed lines between N proteins and RNAs are also similar for both SARS-CoV and SARS-CoV-2. The folding energy and binding energy dependence on pH revealed that the best environment for N proteins to perform their functions with RNAs is the weak acidic environment.
【저자키워드】 COVID-19, SARS-CoV-2, SARS-CoV, protein-protein interactions, protein-RNA/DNA interactions, electrostatic force, DelPhi, DelPhiForce, 【초록키워드】 severe acute respiratory syndrome coronavirus 2, coronavirus, severe acute respiratory syndrome Coronavirus, RNAs, binding energy, Computational approaches, RNA, Spread, Protein, Health, stability, nucleocapsid, N protein, understanding, respiratory, mechanism, function, binding, structures, best, identity, acute respiratory syndrome, Acidic, positive, N proteins, directions, SARS-CoV N protein, develop, affecting, increasingly, the N protein, the SARS-CoV-2, treatments for COVID-19, 【제목키워드】 nucleocapsid protein, feature,