DIPOLES OF THE ALPHA-HELIX AND BETA-SHEET - THEIR ROLE IN PROTEIN FOLDING

As a result of the regular arrangement of peptide dipoles in secondary structure segments and the low effective dielectric constant in Hydrophobic cores, the electrostatic energy of a protein is very sensitive to the relative orientation of the segments. We provide here evidence that the alignment of secondary structure dipoles is significant in determining the three-dimensional structure of globular proteins.