Table 3.
List of RelA‐associated inhibitor (RAI) mutants used in this study
| Mutant | AA position | AA (wild type) | AA (mutant) | AA (p53) | Force |
|---|---|---|---|---|---|
| RAI‐m1 | 773 | Phe | Ala | Met or Ile † | HYD |
| RAI‐m2 | 775 | Asp | Ala | Arg | ION |
| RAI‐m3 | 775 | Asp | Arg | Arg | ION |
| RAI‐m4 | 769 | Tyr | Ala | Arg | HB |
| RAI‐m5 | 795 | Glu | Ala | Arg | ION |
| RAI‐m6 | 795 | Glu | Arg | Arg | ION |
| RAI‐m7 | 769 | Tyr | Ala | Arg | HB |
| 775 | Asp | Ala | Arg | ION |
†
The 773F amino acid of RAI is predicted to interact with three amino acid residues, 243Met, 246Met, and 251Ile, of p53 via hydrogen bonding. AA, amino acid; HB, hydrogen bonding; HYD, hydrophobic interaction; ION, ionic interaction.