title: On the interactions of charged side chains with the alpha-helix backbone.
abstract: The effects of the position of charged amino acid side chains on the stability of the alpha-helix are investigated. Calculations for the model polyAla 13 residue alpha-helix, with modifications based on experimental work, are performed at three levels of approximation. The observed stabilization of the alpha-helix could be explained by interactions between its macrodipole and charged amino acid side chains. Limitations of the model are discussed.
authors.affiliation: Department of Biophysics, Institute, University of Warsaw, Poland.
authors.forename: A
authors.initials: A
authors.lastname: Godzik
authors.forename: T
authors.initials: T
authors.lastname: Wesolowski
mesh_terms: D000596:Amino Acids; D002151:Calorimetry; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins
chemical_list: D000596:Amino Acids; D011506:Proteins