Modeling of the thermal properties of SARS-CoV-2 S-protein

We calculate the thermal and conformational states of the spike glycoprotein (S-protein) of SARS-CoV-2 at seven temperatures ranging from 3 degrees C to 95 degrees C by all-atom molecular dynamics (MD) mu s-scale simulations with the objectives to understand the structural variations on the temperatures and to determine the potential phase transition while trying to correlate such findings of the S-protein with the observed properties of the SARS-CoV2. Our simulations revealed the following thermal properties of the S- protein: 1) It is structurally stable at 3 degrees C, agreeing with observations that the virus stays active for more than two weeks in the cold supply chain; 2) Its structure varies more significantly at temperature values of 60 degrees C-80 degrees C; 3) The sharpest structural variations occur near 60 degrees C, signaling a plausible critical temperature nearby; 4) The maximum deviation of the receptor-binding domain at 37 degrees C, corroborating the anecdotal observations that the virus is most infective at 37 degrees C; 5) The in silico data agree with reported experiments of the SARS-CoV-2 survival times from weeks to seconds by our clustering approach analysis. Our MD simulations at mu s scales demonstrated the S-protein's thermodynamics of the critical states at around 60 degrees C, and the stable and denatured states for temperatures below and above this value, respectively.