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

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Imani, Zeynab | Mundlapati, V. Rao | Brenner, Valérie | Gloaguen, Eric | Le Barbu-Debus, Katia | Zehnacker, Anne | Robin, Sylvie | Aitken, David, J | Mons, Michel

Edité par CCSD ; Royal Society of Chemistry -

International audience. 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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