Stabilization of α-Helices by Dipole−Dipole Interactions within α-Helices

Abstract

Including solvation effects (in the Poisson−Boltzmann continuum solvent approximation) we report ab initio quantum mechanical calculations (HF/6-31G**) on the conformational energies for adding alanine to the amino or carboxyl terminus of a polyalanine α-helix as a function of helix length N. We find that extending the length of an α-helix increasingly favors the α-helix conformation for adding an additional residue, even in hydrophobic environment. Thus, α-helix formation is a cooperative process. Using charges from the QM calculations, we find that the electrostatic energy dominates the QM results, showing that this increasing preference for α-helix formation results from dipole−dipole interaction within the α-helix. These results provide quantitative preferences and insight into the conformational preferences and kinetics of protein folding.

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