Table I

Hydrodynamic Properties of SMC Proteins

ProteinM kD aa seqS Sved.Rs nmM kD experimf/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
ProteinM kD aa seqS Sved.Rs nmM kD experimf/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.

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