On the interactions of charged side chains with the alpha-helix backbone.
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.
Godzik
A
A
Department of Biophysics, Institute, University of Warsaw, Poland.
Wesolowski
T
T
D000596:Amino Acids; D002151:Calorimetry; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins
D000596:Amino Acids; D011506:Proteins