Non-covalent interactions reveal the protein chain δ conformation in a flexible single-residue model
Résumé
The δ conformation is a local secondary structural feature 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 of this conformation have been limited so far to rigid proline-type models that may over-emphasize the significance of the interaction. We show here that in derivatives of a cyclic amino acid with a sulphur atom in the γ-position, specific sidechain/backbone N-H···S interactions stabilize the δ conformation sufficiently to allow it to compete with classical C5 and C7 Hbonding conformers.
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ChemComm_2023_MMons.pdf (1.32 Mo)
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ChemComm_2023_MMons_SI.pdf (3.84 Mo)
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