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Updated: Jul 18, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Carbohydrate amino acids: the intrinsic conformational preference for a beta-turn-type structure in a carbopeptoid
Rebecca A Jockusch1, Francis O Talbot, Paul S Rogers
1Chemistry Department, Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK. rebecca.jockusch@utoronto.ca
Abstract:
Infrared ion-dip spectroscopy coupled with DFT and ab initio calculations are used to establish the intrinsic conformational preference of the basic structural unit of a peptide mimic, a cis-tetrahydrofuran-based "carbopeptoid" (amide-sugar-amide), isolated at low temperature in the gas phase. The carbopeptoid units form a beta-turn-type structure, stabilized by an intramolecular NH --> O=C hydrogen bond across the sugar ring, thus forming a 10-membered, C10 turn. Despite the clear preference for C10 beta-turn structures in the basic unit, however, the presence of multiple hydrogen-bond donating and accepting groups also generates a rich conformational landscape, and alternative structures may be populated in related molecules. Calculations on an extended, carbopeptoid dimer unit, which includes an alternating amide-sugar-amide-sugar-amide chain, identify conformers exhibiting alternative hydrogen-bonding arrangements that are somewhat more stable than the lowest-energy double beta-turn forming conformer.
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