Table 2.
Samples* | Quench (E) | P values† | Separation, Å | % Monomers‡ | Turnover, min−1§ |
---|---|---|---|---|---|
Purified ATPase (10) | 0.6260 ± 0.0315 | 49.6 ± 1.1 | 0 | 9,690 ± 340 | |
Microsomes (19) | 0.2822 ± 0.0287 | <0.0001 | 63.1 ± 1.2 | 53.3 ± 4.6 | 9,473 ± 397 |
Microsomes, no phalloidin (10) | 0.3378 ± 0.0338 | 60.4 ± 1.1 | 47.6 ± 5.4 | 9,476 ± 420 | |
Microsomes + phalloidin (9) | 0.2202 ± 0.0397 | 0.0183 | 66.7 ± 2.1 | 61.6 ± 6.3 | 9,470 ± 363 |
*Numbers in parentheses are number of FRET experiments. Values given in the table are the means ± standard error of the mean.
†The P values were determined by using an unpaired, one-tailed t-test.
‡ % Monomers were determined by assuming the purified ATPase was 100% dimer and dividing the energy transfer efficiency (E) of the microsomes by E (0.626) of the purified ATPase.
§Turnover values for purified ATPase are the mean ± SD from ref. 16. Turnover values for microsomes are the mean ± SD from three experiments ± phalloidin.