TABLE 1.
Thermodynamic parameters of A-site binding of pept-tRNAa
| pept-tRNA | ΔH° (kcal/mole) | ΔG° (kcal/mole) | ΔS° (cal/mole/°K) | TΔS° (kcal/mole) |
| Y37 (10 mM Mg2+)b | −47 ± 4 | −10.0 ± 0.3 | −120 ± 11 | −37 ± 4 |
| Y37 (6 mM Mg2+) | −47 ± 4 | −8.5 ± 0.3 | −125 ± 11 | −39 ± 4 |
| Y37G | −47 ± 6 | −6.9 ± 0.3 | −128 ± 19 | −40 ± 6 |
| Y37A | −42 ± 2 | −8.6 ± 0.1 | −107 ± 6 | −33 ± 2 |
| Y37U | −15 ± 2 | −8.2 ± 0.1 | −21 ± 6 | −7 ± 2 |
| Y37C | −15 ± 1 | −8.1 ± 0.1 | −22 ± 4 | −7 ± 1 |
| −Y (20 mM Mg2+) | −14 ± 1 | −8.6 ± 0.1 | −15 ± 2 | −5 ± 1 |
| −Y (10 mM Mg2+)b | −14 ± 1 | −7.4 ± 0.1 | −19 ± 2 | −6 ± 1 |
aΔG° values were calculated from Kd values measured at 310°K according to the equation ΔG° = RTlnKd; ΔH° and ΔS° values were determined from the slope and the Y-axis intercept of the log(Kd) versus 1/T plot, respectively (Fig. 3C ▶).
bExtrapolated on the basis of the linear Mg2+ dependence of the respective Kd values (Fig. 5 ▶).