Question #4: You have isolated a mutant form of actin that can bind ATP but not hyrolyze it. Other than that change the

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Question #4: You have isolated a mutantform of actin that can bind ATP but not hyrolyze it. Otherthan that change the overall structure of the mutant form of actinis, for our purposes, identical to the wild-type form ofactin. You start with a solution of your mutant form of actinin which the concentration of your G-actin is 10 µM. You addan excess of ATP and Mg++ and let the reaction reach steadystate. At steady state you measure the amount of F-actin andfind that 95% of the G-actin monomers are now contained in F-actinpolymers. What is the critical concentration for your mutantform of actin?
Question #5: After your solution in theprevious problem reaches steady state you dilute it 10-fold withthe same buffer containing ATP and Mg++ but no actin. Youwait an amount of time that you expect that if any reaction(s)could take place they would have reached completion. At thattime, you measure the amount of G-actin and the amount ofF-actin. What fraction of the actin at steady state will beG-actin and what fraction will be F-actin? Explain yourreasoning.
Question #6: Instead of diluting thesolution in the previous problem 10-fold, you dilute it100-fold. Again, you wait an amount of time that you expectthat if any reaction(s) could take place they would have reachedcompletion. At that time, you measure the amount of G-actinand the amount of F-actin. What fraction of the actin atsteady state will be G-actin and what fraction will beF-actin? Explain your reasoning.
please help with 5 and 6, the answer to 4 is 0.5 micromolar