| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T263 |
0-191 |
Sentence |
denotes |
Since the radius of gyration (RoG) helps us to understand the protein structural compactness, RoG of each complex was monitored and represented in Figure S3A in the Supplementary Information. |
| T264 |
192-432 |
Sentence |
denotes |
The average values of RoG are 29.96 Å, 29.52 Å, 29.60 Å, 29.86 Å, 29.75 Å, 29.88 Å, 29.84 Å, 29.74 Å and 29.86 Å for RdRp complexed with remdesivir, EGCG, TF3, TF2b, TF2a, myricetin, quercetagetin, hesperidin and TF1 respectively (Table 3). |
| T265 |
433-517 |
Sentence |
denotes |
This suggests that the structural compactness remained unchanged during simulations. |
| T266 |
518-712 |
Sentence |
denotes |
Finally, the solvent-accessible surface area (SASA) was also explored, and the time evolution of SASA for four RdRp-polyphenol complexes are shown in Figure S3B in the Supplementary Information. |
| T267 |
713-764 |
Sentence |
denotes |
The average values of SASA are reported in Table 3. |
| T268 |
765-876 |
Sentence |
denotes |
Binding of an inhibitor to the substrate changes SASA and sometimes could greatly affect the protein structure. |
| T269 |
877-1001 |
Sentence |
denotes |
Here, a relatively higher SASA value was obtained for RdRp/TF2b (35462.9 Å2) compared to the other RdRp/inhibitor complexes. |
| T270 |
1002-1079 |
Sentence |
denotes |
On the other hand, the lowest SASA value was noted for RdRp/TF3 (34080.2 Å2). |
| T271 |
1080-1173 |
Sentence |
denotes |
Thus, it can be suggested that the binding of TF3 could potentially reduce protein expansion. |
