Shown below are the binding curves for wild type and mutant forms of myoglobin.

Which of the following can best explain the effect of the mutation on oxygen binding by myoglobin?

Question

Shown below are the binding curves for  wild type  and  mutant  forms of myoglobin. 
  
 Which of the following  can best explain the effect of the mutation  on oxygen binding by myoglobin?

Accepted Answer

The mutant myoglobin has a very similar tertiary structure to wild type myoglobin but subtle structural differences give rise to weaker oxygen binding.

Answer

The mutation changes the oxygen binding of myoglobin so that it is allosteric.

Answer

The mutant can still bind to oxygen but the mutation reduces the number of oxygen molecules that can bind to a molecule of myoglobin.

Answer

The mutant myoglobin has a very similar tertiary structure to wild type myoglobin but subtle structural differences give rise to stronger oxygen binding.

Crowdly

Shown below are the binding curves for wild type and mutant forms of myoglob...

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