Backbone Nitrogen Substitution Restricts the Conformation of Glycine Residues in Protein β-Turns

01 October 2024, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

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.

Keywords

Aza-peptide
Glycine
Protein Structure

Supplementary materials

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Description
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Supplementary Information
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Synthetic methods and characterization data
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