In this experiment, 1 micromolar
mant-GTPgS (a fluorescent, non-hydrolyzable GTP analog) was present and the
concentration of the GTP-binding protein, dynamin, was varied by starting at
high concentrations followed by dilution. The binding curve was fit to the anisotropy
equation (in this case the yield of the fluorophore increased about 2 fold upon
binding). A Kd of 8.3 micromolar was found