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. Author manuscript; available in PMC: 2009 Sep 22.
Published in final edited form as: J Am Chem Soc. 2008 Jul 9;130(27):8847–8855. doi: 10.1021/ja802125x

Table 2.

Apparent Zinc-Binding Dissociation Constants for Peptoids and FRET Efficiencies for the Zinc-Bound State of Peptoidsa

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
a

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.

b

Zinc-binding dissociation constants were obtained from the competition assay with EGTA (Figure 6).