title: Tests of the helix dipole model for stabilization of alpha-helices.
abstract: Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm-Bragg model for alpha-helix formation.
mesh_terms: D000595:Amino Acid Sequence; D002096:C-Peptide; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011487:Protein Conformation; D013696:Temperature
chemical_list: D002096:C-Peptide