The conformation is a local secondary structure in proteins that implicates a π N-H⋯N interaction between a backbone N atom and the NH of the following residue. Small-molecule models thereof have been limited so far to rigid proline-type compounds. We show here that in derivatives of a cyclic amino acid with a sulphur atom in the γ-position, specific side-chain/backbone N-H⋯S interactions stabilize the conformation sufficiently to allow it to compete with classical C5 and C7 H-bonded conformers.

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http://dx.doi.org/10.1039/d2cc06658kDOI Listing

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