Trapping a folding intermediate of the alpha-helix: stabilization of the pi-helix.
Amino Acid Sequence
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
We report the design, synthesis, and characterization of a short peptide trapped in a pi-helix configuration. This high-energy conformation was nucleated by a preorganized pi-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the pi-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.