This work shows that hybrid peptides formed by alternating trans-2-aminocyclopentanecarboxylic
acid (trans-ACPC) and trans-2-aminocyclohexanecarboxylic acid (trans-ACHC) do not
fold in the solvents typically used in the study of their homo-oligomers. Only when
the peptides are assayed in SDS micelles are the predicted helical structures obtained.
This indicates that the environment could play an equally important role (as the backbone
stereochemistry) in determining their fold, possibly by providing a sequestered environment.