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You have isolated a mutant form of actin that can bind to ATP but not hydrolyze it. Other than that change the overall structure of the mutant form of actin is, for our purposes, identical to the wild-type for of actin. You start with a solution of your mutant form of actin in which the concentration of your G-actin is 10 microM. You add excess of ATP and Mg++ and let the reaction reach steady state. At steady state you measure the amount of F-actin and find that 95% of the G-actin monomers are now contained in F-actin polymers. What is the critical concentration for your mutant form of actin?
After your solution in the previous problem reaches steady state you dilute it 10-fold with the same buffer containing ATP and Mg++ but no actin. You wait an amount of time that you expect that if any reaction could take place they would have reached completion. At that time, you measure the amount of G-actin and the amount of F-actin. What fraction of the actin at steady state will be G-actin and what fraction will be F-actin. Explain your reasoning
Is the amount you calculated a plausible amount of sample to put on a plate?
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