| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T254 |
0-102 |
Sentence |
denotes |
Hydrophobic interactions also play an important role in stabilizing the RBD/ACE2 complex in nCOV-2019. |
| T255 |
103-223 |
Sentence |
denotes |
An important interaction between nCOV-2019 RBD and ACE2 is the π-stacking interaction between F486 (RBD) and Y83 (ACE2). |
| T256 |
224-326 |
Sentence |
denotes |
This interaction helps in stabilizing L3 in nCOV-2019 compared to SARS-COV where this residue is L472. |
| T257 |
327-473 |
Sentence |
denotes |
It was observed by Gao et al.26 that mutation L472 to F486 in nCOV-2019 results in a net change in the binding free energy of −1.2 ± 0.2 kcal/mol. |
| T258 |
474-613 |
Sentence |
denotes |
Other interfacial residues in nCOV-2019 RBD that participate in the hydrophobic interaction with ACE2 are L455, F456, Y473, A475, and Y489. |
| T259 |
614-703 |
Sentence |
denotes |
It is interesting to note that all these residues except Y489 have mutated from SARS-COV. |
| T260 |
704-956 |
Sentence |
denotes |
Spinello and co-workers30 performed long-timescale (1μs) simulation of nCOV-2019/ACE2 and SARS-COV ACE2 and found that L3 in nCOV-2019 is more stable due to presence of the β6 strand and existence of two H-bonds in L3 (H-bonds G485-C488 and Q474-G476). |
| T261 |
957-1132 |
Sentence |
denotes |
Importantly, an amino acid insertion in L3 makes this loop longer than L3 in SARS-COV and enables it to act like a recognition loop and make more persistent H-bonds with ACE2. |
| T262 |
1133-1293 |
Sentence |
denotes |
L455 in nCOV-2019 RBD is important for hydrophobic interaction with ACE2 and mutation L455A lowers the vdw contribution of binding affinity by about 5 kcal/mol. |
| T263 |
1294-1367 |
Sentence |
denotes |
The H-bonds between RBD of nCOV-2019 and SARS-COV are shown in Figure 9A. |
| T264 |
1368-1491 |
Sentence |
denotes |
The structural details discussed here are in agreement with other structural studies of the nCOV-2019 RBD/ACE2 complex.4,53 |
