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Further studies of the helix dipole model: Effects of a free α‐NH3+ or α‐COO− group on helix stability

Interactions between the α‐helix peptide dipoles and charged groups close to the ends of the helix were found to be an important determinant of α‐helix stability in a previous study.1 The charge on the N‐terminal residue of the C‐peptide from ribonuclease A was varied chiefly by changing the α‐NH2 blocking group, and the correlation of helix stability with N‐terminal charge was demonstrated. An alternative explanation for some of those results is that the succinyl and acetyl blocking groups stabilize the helix by hydrogen bonding to an unsatisfied main‐chain NH group. The helix dipole model is tested here with peptides that contain either a free α‐NH  3+ α‐COO− groups, and no other charged groups that would titrate with similar pKa's. This model predicts that α‐NH3α‐COO‐ groups are helix‐destabilizingand that the destabilizing interactions are electrostatic in origin. The hydrogen bonding model predicts that α‐NH3 and α‐COO‐ groups are not themselves helix‐destabilizing, but that an acetyl or amide blocking group at the N‐ or C‐ terminus, respectively, stabilizes the helix by hydrogen bonding to an unsatisfied main‐chain NH or CO group.