Table 1.
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 |
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.
Estimated by extrapolation to saturation conditions from the experimental data of Ni et al.29
1/(τbound + τunbound)
1/(<tbound> + <tunbound>
Estimated from ligand exchange with AMP-PNP.