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Stopped-flow kinetic binding measurements of Max, Myc and Mad to FITC labeled Max protein. Representative kinetic data show the time dependent increase in anisotropy after mixing 50 nM FITCMax (final concentration) with 0.2 µM unlabeled (final concentration) of (A) Myc, (B) Mad and (C) Max at 21°C. Residuals for the fits are shown in the lower panels. The experimental conditions are described under “Experimental Procedures”.
