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Independent of the ring size in the aliphatic side chains, peptides made up of β2,3-cyclic aminoxy acids, novel chiral building blocks of foldamers, adopt uniform secondary structures consisting of rigid β NO turns and 1.89-helix structures (see figure). This contrasts previous results from other groups with cyclic ring-constrained β-peptides.
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Yang et al. (2004) studied this question.
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