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. Author manuscript; available in PMC: 2021 Mar 17.
Published in final edited form as: Biochemistry. 2020 Feb 27;59(10):1104–1112. doi: 10.1021/acs.biochem.9b01038

Table 2.

RecA3 G4 binding by Biolayer Interferometry

KD (nM) Ka (1/Ms) x104 Ka Error (1/Ms) x104 Kd (1/s) X10−3 Kd error (1/s) x10−3
Parental T:TT:T 35.1 12.3 0.4 4.30 0.14
T:TT:AT 49.2 10.3 0.3 5.02 0.15
A:AA:A 114 8.88 0.54 10.1 1.0
AT:ATT:AT 366 1.79 0.11 6.53 0.25
TTT:GC:ATC 485 1.95 0.23 9.43 0.59
G4 Mutant 291 3.32 0.38 9.65 0.56

KD was determined by determining the binding kinetics using between six and eight different RecA3 concentrations and analyzing the KD using the global fitting analysis to binding curves (Figure S4). At least three protein concentrations were analyzed above and below the apparent KD for each sample. Ka= association rate, Kd = disassociation rate, KD = disassociation constant