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Protein Y is a globular protein that normally assembles as a tetramer.You are examining the interactions between the subunits by changing the amino acids on the surface of the protein.You compare the wild-type (nonmutated) protein and a mutant version with a single amino acid substitution.When washed through the same gel-filtration column, mutant protein Y runs through the column more slowly than the normal protein.Which of the following changes in the mutant protein is most likely to explain this result? Explain your choice.
A.the loss of a binding site on the mutant-protein surface through which protein Y normally forms dimers
B.a change that results in the mutant protein acquiring an overall positive instead of a negative charge
C.a change that results in the mutant protein being larger than the wild-type protein
D.a change that results in the mutant protein having a slightly different shape from the wild-type protein
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