Table 1. Protein Capture by YaxAΔ40B80a.
| protein | mass (kDa) | rh (Å) | IRES ± σ (%) | σblockade ± σ | kon (μM–1 s–1) | koff (s–1) |
|---|---|---|---|---|---|---|
| CRP49 in buffer | 125 (pentamer) | 43.74 | 79.7 ± 2.1 | 1.4 ± 0.2 | 308.9 ± 9.7 | 27.0 ± 0.7 |
| CRP + serum | 78.9 ± 0.5 | 1.2 ± 0.1 | NDb | 36.8 ± 6.1 | ||
| HG50 | 64 (tetramer) | 33.10 | 56.3 ± 3.6 | 0.95 ± 0.15 | 208.6 ± 8.9 | 189.1 ± 3.9 |
| SA51 | 53 (tetramer) | 31.62 | 47.6 ± 2.9 | 1.1 ± 0.2 | 473.2 ± 16.6 | 13.3 ± 0.3 |
| BT52 | 35 (dimer) | 30.38 | 23.3 ± 3.4 | 1.3 ± 0.1 | 150.9 ± 4.4 | 121 ± 8.7 |
a
Mass and hydrodynamic radius (rh) were computed with HullRad48 software. The error in IRES and σblockade represents the standard deviation (σ) of cumulated data points (n = 1800) from three technical replicates (N = 3 pores). The σblockade is normalized for the noise in the IO. The kon and koff are computed from the capture and release rates shown in Figure S23. Experiments were performed in 150 mM NaCl, 15 mM TrisHCl (pH, 7.5), with 120 nM protein in cis. Data was recorded with 50 kHz sampling rate and 10 kHz low-pass Bessel filter.
b
Note that serum proteins also are captured by the nanopore and interfere with the measurement of kon.