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Non-covalent interactions reveal the protein chain δ conformation in a flexible single-residue model.

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The δ conformation is a local secondary structure in proteins that implicates a πamide N-H⋯N interaction between a backbone N atom and the NH of the following residue. Small-molecule models… Click to show full abstract

The δ conformation is a local secondary structure in proteins that implicates a πamide 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 δ conformation sufficiently to allow it to compete with classical C5 and C7 H-bonded conformers.

Keywords: interactions reveal; conformation; chain; reveal protein; non covalent; covalent interactions

Journal Title: Chemical communications
Year Published: 2023

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