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. Author manuscript; available in PMC: 2010 Sep 29.
Published in final edited form as: Biochemistry. 2009 Sep 29;48(38):9084–9093. doi: 10.1021/bi9010495

Table 1.

Dissociation and Association Rate Constants of Wild-Type RTa

method protein solnsb kdiss, 10−6 s−1 kobs, 10−6 s−1 kass, M−1s−1
dissociation reaction

pre-steady-state assay 50 nM p66/p51 4.4 ± 0.2
Trp fluorescencec 50 nM p66/p51 3.9 ± 0.3

association reaction

pre-steady-state assay 0.5 µM p66, 0.5 µM p51 5.8 ± 0.2 2.2 ± 0.2 d
0.5 µM p66, 2.5 µM p51 7.8 ± 0.3 1.3 ± 0.2 e
1.4 ± 0.2 f
Trp fluorescencec 0.5 μM p66, 0.5 μM p51 5.4 ± 0.4
a

RT buffer D with 1 mM TCEP, 5 °C. Errors are standard deviations of 3–9 experiments

b

Final concentrations

c

λex = 295 nm, λem = 340 nm

d

Calculated from eq 3

e

Calculated from eq 4

f

Calculated from eq 13.