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. Author manuscript; available in PMC: 2014 May 29.
Published in final edited form as: J Am Chem Soc. 2013 May 14;135(21):7861–7868. doi: 10.1021/ja311604j

Table 1.

PKA binding rates.a

Single-Molecule Ensemble
ATP τ ± σ <t> ± σ <t>
bound (ms) 1.99 ± 0.03 3.1 ± 4.3 5.329
unbound (ms) 0.77 ± 0.01 5.0 ± 19 > 0.25b
binding / unbind-
ing cycle (s−1)
362c ± 5 125d < 190b,e

Kemptide τ ± σ <t> ± σ <t>
bound (ms) 0.77 ± 0.01 1.8 ± 2.9 <230
Unbound (ms) 0.67 ± 0.01 1.7 ± 3.7 <2017
binding / unbind-
ing cycle (s−1)
696c ± 8 286d >46
a

Where τ is the characteristic time from an exponential fit to the data reported in Figure 3, and <t> is the arithmetic mean from the distribution shown in Figure 3.

b

Estimated by extrapolation to saturation conditions from the experimental data of Ni et al.29

c

1/(τbound + τunbound)

d

1/(<tbound> + <tunbound>

e

Estimated from ligand exchange with AMP-PNP.