Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a versatile method for studying folding in peptides, proteins, and their mimetics. In natural entities, the straightforward to obtain metric of proton chemical shift provides residue‐level insights into folded structure as well as dynamics. Rao et al. report the expansion of such methods to protein‐like chains with non‐canonical backbone compositions. Comparison of the NMR properties of a library of artificial residues in random coil and helical contexts reveals systematic chemical shift changes associated with certain residues adopting a helical folded conformation. (doi: 10.1002/pep2.24297) image
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