Backbone nitrogen substitution restricts the conformation of glycine residues in β-turns
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.
Authors
- Diana Thomas (ORCID: https://orcid.org/0009-0000-4963-8978)
- Robert W. Newberry (ORCID: https://orcid.org/0000-0002-2020-2641)
- Fengyi Gu (ORCID: https://orcid.org/0009-0002-7437-4876)
Institutions
- The University of Texas at Austin (US)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-12-01
- DOI
- https://doi.org/10.1039/d5cc06335c
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00