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.

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Publication Details

Journal
Chemical Communications
Published
2025-12-01
DOI
https://doi.org/10.1039/d5cc06335c
Primary Topic
Chemical Synthesis and Analysis
Type
article
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article

Backbone nitrogen substitution restricts the conformation of glycine residues in β-turns

Diana Thomas, Robert W. Newberry, Fengyi Gu
Chemical Communications
Chemical Synthesis and Analysis
article

Backbone nitrogen substitution restricts the conformation of glycine residues in β-turns

Diana Thomas, Robert W. Newberry, Fengyi Gu
article en

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.

Chemical CommunicationsVol. 62(1)
The University of Texas at Austin (US)
Openalex Percentile: Top 66%
Chemical Synthesis and Analysis
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