Hydrodynamic Properties of SMC Proteins
| Protein . | . | M kD aa seq . | . | S Sved. . | . | Rs nm . | . | M kD experim . | . | f/fmin . |
|---|---|---|---|---|---|---|---|---|---|---|
| BsSMC | 2 × 135 | 6.3 | 10.3 | 269 | 2.5 | |||||
| BsSMCΔN* | 2 × 117 | 6.1 | 2.3 | |||||||
| XCAP-C/E | 147 + 136 | 8 | 2.0 | |||||||
| MukB | 2 × 170 | 9.6 | 7.6 | 328 | 1.9 | |||||
| FN-MukBcoil | 2 × 133 | 7.0 | 9.6 | 272 | 2.3 |
| Protein . | . | M kD aa seq . | . | S Sved. . | . | Rs nm . | . | M kD experim . | . | f/fmin . |
|---|---|---|---|---|---|---|---|---|---|---|
| BsSMC | 2 × 135 | 6.3 | 10.3 | 269 | 2.5 | |||||
| BsSMCΔN* | 2 × 117 | 6.1 | 2.3 | |||||||
| XCAP-C/E | 147 + 136 | 8 | 2.0 | |||||||
| MukB | 2 × 170 | 9.6 | 7.6 | 328 | 1.9 | |||||
| FN-MukBcoil | 2 × 133 | 7.0 | 9.6 | 272 | 2.3 |
“M kD aa seq” is the mass calculated for the presumed dimer from the aa sequence. S and Rs were experimentally determined as described, and “M experim” was calculated from these values (Siegel and Monte, 1966). f/fmin is the ratio of the experimental frictional coefficient (determined from S) to that of an unhydrated sphere of the same mass.
BsSMC with the NH2-terminal domain truncated.