ArticleChemical communications (Cambridge, England)2026
Backbone nitrogen substitution restricts the conformation of glycine residues in β-turns.
Article in Chemical communications (Cambridge, England), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
3 authors.
Funding
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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Registered trials
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