Backbone nitrogen substitution restricts the conformation of glycine residues in β-turns
Fengyi Gu1, Diana Thomas1, Robert W Newberry1
1Department of Chemistry, The University of Texas at Austin, 105 E. 24th St., Austin, TX, 78712, USA. rnewberry@utexas.edu.
Abstract:
Glycine adopts backbone conformations that are generally inaccessible to other amino acids, but specifying a particular conformation remains challenging. Inspired by studies of small-molecule models, we hypothesized that substituting the alpha carbon with nitrogen would bias glycine toward specific β-turn conformations, which we confirmed through biophysical analysis of backbone-modified peptides.
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