On the interactions of charged side chains with the alpha-helix backbone
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
1Department of Biophysics, Institute, University of Warsaw, Poland.
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.
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