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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 2.

Dissociation and Association Rate Constants of Labeled RTa

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

50 nM p66-A488/p51-QSY9 2.5 ± 0.5
50 nM p66-QSY9/p51-A488 1.9 ± 0.4

association reaction

0.5 µM p66-A488, 0.5 µM p51-QSY9 4.1 ± 0.4
0.5 µM p66-QSY9, 0.5 µM p51-A488 3.4 ± 0.4
0.5 µM p66-A488, 1.5 µM p51-QSY9 4.8 ± 0.3 1.6 ± 0.2
0.5 µM p66-A488, 2.0 µM p51-QSY9 5.7 ± 0.4 1.6 ± 0.2
0.5 µM p66-A488, 2.5 µM p51-QSY9 7.1 ± 0.3 1.8 ± 0.4
a

RT buffer D, 5 °C. Errors are standard deviations of 3 experiments. λex = 450 nm, λem = 520 nm

b

Final concentrations

c

Calculated from eq 13.