Table 2. The strong interactions in the hydrophobic core that are responsible for maintaining insulin in its closed conformation.
Interaction | Distance in the crystal structure [Å] | Average distance during MD simulations where insulin stays at its closed conformation [Å] |
---|---|---|
F24(Aromatic)–L15(C) | 5.2 | 4.6±0.5 |
Y26 (Aromatic)–I2A(C) | 5.2 | 5.5±2.1 |
Y26(Aromatic)–L11(C) | 5.2 | 5.8±1.3 |
Y26(Aromatic)–V12(C) | 3.8 | 4.5±1.0 |
The distances were calculated from the center of the benzene ring (aromatic) to the nearest C atom. The same trajectory data as in Table 1 were used in calculating the average distances.