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Table 2 Apparent affinities of nucleotides in F 2 FlAsH-αβγM complexes

From: Biarsenical ligands bind to endogenous G-protein α-subunits and enable allosteric sensing of nucleotide binding

 

pEC50a

 

GTPγS

GppNHp

GDP

GMP

αslong

7.47 ± 0.09

6.56 ± 0.07

4.72 ± 0.18

ND

αsshort

7.06 ± 0.04

6.42 ± 0.04

4.85 ± 0.05

< 3

α13

5.65 ± 0.13

5.36 ± 0.14

4.98 ± 0.23

ND

αq

6.27 ± 0.05

5.96 ± 0.07

5.87 ± 0.06

< 3

αolf

6.43 ± 0.04

5.84 ± 0.05

5.00 ± 0.03

< 3

αi1

8.19 ± 0.05

8.08 ± 0.04

8.19 ± 0.16

5.89 ± 0.12

αi2

8.02 ± 0.09

7.84 ± 0.14

8.17 ± 0.13

4.45 ± 0.07

αi3

7.87 ± 0.06

7.93 ± 0.07

8.08 ± 0.10

5.29 ± 0.13

  1. anegative logarithm of concentration of the nucleotide causing 50% of fluorescence anisotropy changes of F2FlAsH-αβγM complexes (mean ± SD), determined after 6 h incubation for αslong, αsshort, αq and αolf, after 14 h for α13, after 2 h for αi1, αi2 and αi3.
  2. Data is from two to three independent experiments carried out in duplicate. Data were pooled and then fitted to three parameter competitive binding equations.