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The data below shows four different protein unfolding curves for the same protein but containing various mutations.
The protein is 280 amino acids long. The N-terminal region of the protein involves a cluster of hydrophobic amino acids critical for stabilising the overall structure of the protein. The C-terminal region contains a solvent-exposed pocket containing charged amino acids that, whilst not so critical for protein folding, play an important role in the protein's function.
The mutations studied were as follows:
The wild-type (WT) version of the protein has been extensively studied and no mutation has ever been found that has improved stability.
Which condition corresponds to which version of the protein?