Table 3.
Characteristics of N50‐Imp α Interactions
| Imp α1 | Imp α5 | |||
|---|---|---|---|---|
| Major | Minor | Major | Minor | |
| A. VQRKRQKLMP | ||||
| KD (BLI), nmol/L | N/D | N/D | 73 | 140 |
| B. QRKRQK | ||||
| ΔG (dock), kcal/mol | −6.6 | −6.1 | −7.3 | −6.9 |
| KD (calc)*, nmol/L | 4.5 | 19 | 0.6 | 1.9 |
| C. QRDEQK | ||||
| ΔG (dock), kcal/mol | −6.3 | −6.3 | −6.2 | −6.2 |
| KD (calc)*, nmol/L | 11 | 11 | 15 | 15 |
A, N50‐Imp α binding affinity (KD) obtained from Bio‐Layer Interferometry (see Figure 6), B and C, Docking energy and calculated docking affinity obtained from modeling of B, N50 and C, N50M interactions with Imp α1 and α5. Docking energy was generated by AutoDock Vina 1.1.2. Please note that docking affinities obtained from the modeling study differ from those obtained from BLI due to different experimental conditions (temperature, ligand size, etc.). However, the binding characteristics are generally consistent between the 2 methods.
*
Calculated from the equation ΔG=RT·ln(KD) for T=173 K, with the assumption that rotation around the majority of bonds is frozen.