Related Experiment Video
Updated: Jul 5, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Residue requirements for helical folding in short alpha/beta-peptides: crystallographic characterization of the
Margaret A Schmitt1, Soo Hyuk Choi, Ilia A Guzei
1Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Abstract:
Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both alpha-amino acid and beta-amino acid substitution on alpha/beta-peptide helicity. We also report the first X-ray crystal structure of a helical alpha/beta-peptide. We conclude that a certain amount of conformational preorganization in alpha/beta-peptides (via the inclusion of constrained beta-amino acids or alpha,alpha-disubstituted alpha-amino acids) is needed to promote helical folding; acyclic beta-amino acids and beta-branched alpha-amino acids are tolerated to only a limited extent.
Related Concept Videos
Structures of Solids
Newman Projections
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as conformers.
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Crystallographic Point Groups
Imperfections in Crystal Structure: Stoichiometric Point Defects
Imperfections in Crystal Structure: Non-Stoichiometric Defects

