| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T364 |
0-90 |
Sentence |
denotes |
Additional sequence differences between nCOV-2019 and SARS-COV influence RBD/ACE2 binding. |
| T365 |
91-291 |
Sentence |
denotes |
Residue D480 in SARS-COV contributes negatively to total binding energy (6.25 ± 0.14 kcal/mol) and mutating this residue to S494 in nCOV-2019 lowers this negative contribution to 1.17 ± 0.06 kcal/mol. |
| T366 |
292-396 |
Sentence |
denotes |
D480 in SARS-COV is located in a region of high negative charge from residues E35, E37, and D38 on ACE2. |
| T367 |
397-572 |
Sentence |
denotes |
Electrostatic repulsion between D480 on SARS-COV and the acidic residues on ACE2 is the reason for highly negative contribution of this residue to binding of SARS-COV to ACE2. |
| T368 |
573-649 |
Sentence |
denotes |
Mutation to S494 in this location removes this highly negative contribution. |
| T369 |
650-812 |
Sentence |
denotes |
Gao and co-workers26 computed the relative free energies of binding because of mutations from the RBD-ACE2 of SARS-COV to the corresponding residues in nCOV-2019. |
| T370 |
813-971 |
Sentence |
denotes |
They used a FEP approach and showed that mutation D480S in SARS-COV changed the binding free energy by −1.9 ± 0.8 kcal/mol which is consistent with our study. |
| T371 |
972-1193 |
Sentence |
denotes |
Furthermore, we performed an additional simulation on D480A mutant in SARS-COV and found that this mutation has a binding affinity of 23.46 ± 3.07 kcal/mol which is about 5 kcal/mol higher than the wild-type SARS-COV RBD. |
| T372 |
1194-1379 |
Sentence |
denotes |
In addition, experimental binding affinity measurements showed that mutations of S494 to an acidic residue highly reduce the binding affinity to ACE2 which confirms the hypothesis here. |
