Table 2.
peptoid | apparent kd (M) | ΔΔGzn (kcal/mol) | FRET efficiency |
---|---|---|---|
2_FQ | (1.2 ± 0.5) × 10−6 | 0 | 0.86 ± 0.01 |
3_FQ | (5.8 ± 1.0) × 10−6 | 0.9 | 0.85 ± 0.01 |
4_FQ | (8.9 ± 2.2) × 10−6 | 1.0 | 0.68 ± 0.01 |
5_FQ | (6.5 ± 1.4) × 10−6 | 1.2 | 0.78 ± 0.01 |
6_FQ | (8.5 ± 3.0) × 10−5 | 2.5 | 0.66 ± 0.02 |
7_FQ | (3.7 ± 1.5) × 10−6 | 0.7 | 0.79 ± 0.01 |
8_FQ | ∼0.3 × 10−9 b | −4.9 | 0.88 ± 0.01 |
9_FQ | ∼0.4 × 10−9 b | −4.7 | 0.81 ± 0.02 |
11_FQ | (8.9 ± 3.4) × 10−7 | −0.2 | 0.77 ± 0.01 |
12_FQ | (7.8 ± 2.8) × 10−7 | −0.3 | 0.68 ± 0.01 |
The free energy difference of the zinc-bound state (ΔΔG zn) was calculated from ΔΔG zn = −RT ln (kd_ref/kd_sample). R is the gas constant and T is temperature. We took the kd of 2_FQ as the reference kd.
Zinc-binding dissociation constants were obtained from the competition assay with EGTA (Figure 6).