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Figure 3


Fig. 3. Interactions of wild-type Srv2 and mutants Srv2-201, Srv2-202 and Srv2-203 with ADP-G-actin. An increase in the fluorescence of 0.2 µM NDB-labeled G-actin was measured under physiological salt conditions at pH 8.0. Dissociation constants were calculated from the binding curves. Srv2, Srv2-201 and Srv2-203 bound to actin monomers with high affinity (KD=0.066 µM, 0.056 µM and 0.074 µM, respectively), whereas Srv2-202 bound actin monomers with considerably lower affinity (KD=0.4 µM).





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