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Keywords:

  • biophysics;
  • foldamers;
  • peptides;
  • protein folding;
  • thioesters
Thumbnail image of graphical abstract

Backbone thioester exchange is used to explore a fundamental type of protein–foldamer packing motif, the association of an α helix and an α/β-peptide foldameric helix, which is analogous to an antiparallel coiled-coil tertiary structure in a pure α-residue backbone. Side-chain packing preferences at this chimeric tertiary interface are comparable to those that determine pairing propensities among antiparallel α helices.