The protein below has all of the following EXCEPT

In the context of protein structure, α-helices are a common secondary structure formed through hydrogen bonds between the backbone amide and carbonyl groups. The nature of α-helices is that they are typically right-handed in configuration, meaning they twist in a clockwise direction when viewed from the N-terminus to the C-terminus. Left-handed α-helices do exist, but they are extremely rare and not commonly found in the context of regular protein structure.

The presence of right-handed α-helices, β-sheets, and disulfide bonds is typical in many proteins. Right-handed α-helices are prevalent, β-sheets are another important form of secondary structure that allows proteins to be stabilized through hydrogen bonding between different strands, and disulfide bonds contribute to the stability of a protein's tertiary structure by forming covalent links between cysteine residues.

Thus, stating that the protein has left-handed α-helices is indeed the accurate point of exclusion, as these are not generally found within the standard configurations of most proteins and are not part of the common protein configurations seen in biological systems.