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You are investigating the folding kinetics of a protein involved in the cell cyc

ID: 42012 • Letter: Y

Question

You are investigating the folding kinetics of a protein involved in the cell cycle. From your previous equilibrium experiments, you know that the CM (concentration of dénaturant at which half the protein is folded and half is unfolded) is ~2.75 M. Below CM, you measure the rate of folding by taking the unfolded protein in denaturant solution and diluting it in buffer. Above CM, you measure the rate of unfolding by taking the folded protein in buffer and diluting it in denaturant solution. You extract the observed rate constants kobs, where kobs= kfold+kunfold, from these experiments and plot them all on the same graph: A mutant form of the protein associated with carcinogenesis is more stable and has CM=4. You repeat the same experiments as above with this mutant protein and find that it has the same unfolding rate constant as the wild type protein, but that its folding rate constant is altered. Would the folding rate constant be greater than or less than that of the wild type protein? Explain your answer.

Explanation / Answer

The folding rate constant will be less than less than that of wild type protein because in the mutant form the protein is more stable when associated with carcinogenesis.

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