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. Author manuscript; available in PMC: 2008 Nov 25.
Published in final edited form as: Biochemistry. 2008 Mar 8;47(13):4181–4188. doi: 10.1021/bi701769u

Figure 3.

Figure 3

Kinetics of Tβ4 binding to actin. (A) Time courses of 5 (a), 10 (b) and 25 μM Tβ4 (c) (P4A mutant shown) binding to 0.5 μM AEDANS-actin monomers. The inset shows time courses of 0.2 μM Alexa-S43C Tβ4 binding to unlabeled 4 (a) and 25 μM actin monomers (b). The solid lines through the data are the best fits to single exponentials. (B) Tβ4 concentration dependence of the observed association rate constants: (●) wild-type, (◆) P4A, (■) L28A, (▲) I34A, and (○) Alexa-Tβ4. (C) Tβ4 concentration dependence of the observed association rate constants of K18A/K19A Tβ4 binding to actin monomers. Symbols represent data acquired on two separate days using two different preparations. Error bars represent standard errors in the best fits of the time courses to single exponentials.