. 2024 Jun 4;10(6):1262–1275. doi: 10.1021/acscentsci.4c00314

Table 2. Kinetic and Thermodynamic Parameters for aa-tRNA^Phe Binding to EF-Tu-LD655 in the Presence and Absence of EF-Ts from the Experiments in Figure 3 ^a.

rate constant	l-α-Phe		(S)-β³-Phe
EF-Ts	–	+	–	+
k_on (μM^–1 s^–1)	5.0 ± 0.1	8.0 ± 0.3	1.0 ± 0.1	3.0 ± 0.3
k_off (s^–1)	0.2 ± 0.1	0.8 ± 0.2	1.0 ± 0.1	1.8 ± 0.2
K_D (est.)	40 nM	100 nM	1 μM	0.6 μM
ΔG° (kcal/mol)	–11.5	–9.6	–4.1	–4.4

K_D values were estimated from the ratio K_D = k_off /k_on, determined from titration experiments in Figure 3. Free energies were calculated using the relationship ΔG° = –RT ln(1/K_D)²¹.

Table 2. Kinetic and Thermodynamic Parameters for aa-tRNAPhe Binding to EF-Tu-LD655 in the Presence and Absence of EF-Ts from the Experiments in Figure 3a.

Table 2. Kinetic and Thermodynamic Parameters for aa-tRNA^Phe Binding to EF-Tu-LD655 in the Presence and Absence of EF-Ts from the Experiments in Figure 3 ^a.