Table 1.
Thermodynamic Data for Q7 Binding
| guest | Kd (nM)d | ΔHd (kcal mol−1) |
−TΔSe (kcal mol−1) |
|---|---|---|---|
| AM-insulin | 99 (±6) | −15.2 (±0.1) | 5.6 (±0.9) |
| insulina | 670 (±160) | −10.8 (±0.5) | 2.3 (±0.4) |
| change due to AMb | 6.8-fold | −4.4 | 3.3 |
| Amf-Gly-Glyc | 0.95 (±0.15) | −14.2 (±0.2) | 1.8 (±0.2) |
| Phe-Gly-Glyc | 310 (±80) | −13.4 (±0.4) | 4.4 (±0.3) |
| change due to AMb | 330-fold | −0.8 | −2.6 |
| Gly-Amf-Glyc | 510 (±20) | −8.2 (±0.1) | −0.5 (±0.1) |
| Gly-Phe-Glyc | 4300 (±100) | −9.8 (±0.1) | 2.4 (±0.1) |
| change due to AMb | 8.4-fold | 1.6 | −2.9 |
| AM-phenylalaninec | 460 (±10) | −4.2 (±0.1) | −4.5 (±0.1) |
| phenylalaninec | 8700 (±1100) | −7.6 (±0.2) | 0.7 (±0.1) |
| change due to AMb | 41-fold | 3.4 | −5.2 |
a
Data from ref 7.
b
Change due to aminomethylation was calculated as the quotient of Kd values or the difference in ΔH or −TΔS values.
c
Data from ref 9.
d
Mean values measured from at least three ITC experiments at 300 K in 10 mM sodium phosphate, pH 7.0.
e
Entropic contributions to the free energy of binding were calculated from the Kd and ΔH values, with error values propagated from those of Kd and ΔH.