TABLE 2.
Membrane binding properties of BAR domains and mutants
| Proteins |
Kda |
πcb |
||
|---|---|---|---|---|
| POPC/POPS (80:20) | POPC/POPS/PtdIns(4,5)P2 (77:20:3) | POPC/POPS (80:20) | POPC/POPS/PtdIns(4,5)P2 (77:20:3) | |
| nm | dynes/cm | |||
| dAmp-BAR WT | 300 ± 60 | 105 ± 20 | 28 ± 0.4 | 32 ± 0.5 |
| dAmp-BAR-ΔH0 | NMc | NM | 28 ± 0.5 | 28 ± 0.4 |
| dAmp-BAR K137A/R138A/R140A/K141A | 2000 ± 100 | 400 ± 60 | 27 ± 0.6 | 31 ± 0.5 |
| EndoA1-BAR WT | 100 ± 20 | 30 ± 8 | 32 ± 0.4 | 35 ± 0.5 |
| EndoA1-BAR-ΔH0 | 2000 ± 300 | 1900 ± 300 | 30 ± 0.3 | 30 ± 0.3 |
| EndoA1-BAR-ΔHi | NM | 100 ± 20 | 28 ± 0.3 | 33 ± 0.4 |
| EndoA1-BAR K171A/K172A/K173A/R174A | 300 ± 60 | 90 ± 10 | 31 ± 0.4 | 34 ± 0.3 |
a Determined by the curve fitting of binding isotherms derived from equilibrium SPR sensorgrams. Mean ± S.D. values were determined from >3 separate measurements.
b Determined by the extrapolation of the Δπ versus π0 plot of the monolayer measurements to the abscissa (see Fig. 3). Mean ± S.D. values were determined from triplicate measurements.
c NM, not measurable.