Xeno amino acid peptide: MD with NOE restraints

For full details, see the manuscript. Using NMR-informed molecular dynamics, we have observed a propensity towards a short β-bend at the N-terminus (residues v3-a5) and an α-helical structure at the C-terminus (residues a18-a24). The φ and ψ dihedral angles of these residues in 10 representative structures from independent MD replicas suggest a mix of C-terminal α-helix and N-terminal β-bend, except for MD replicate number 4, the least stable structure, where we observe a shorter C-terminal α-helix starting at n20. P2 is thus the first peptide constructed entirely from a xeno amino acid alphabet that has been observed to adopt any secondary structure elements according to CD, MD, and NMR.