Abstract
The structure of unnatural hexapeptides containing three L-valine units and three unnatural α-amino acids ((2R)-methyl aspartic acid, (2S)-methylornitine and modified proline) has been elucidated using 1H-NMR and IR spectroscopy and conformational analysis based on molecular dynamics (MD) and cluster analysis. The MD analysis, which provides conformer populations and hydrogen-bond lifetimes, is in good agreement with the 1H-NMR and IR data.
†See Refs. [16,17,18] for Parts 1, 2 and 3, respectively.
Acknowledgements
The authors are grateful to Professor Sergio Sandri for helpful advice and discussions. The authors are also grateful to the University of Bologna (Ricerca Fondamentale Orientata, ex 60%) and the CINECA computer centre of Bologna for financial support.
Notes
†See Refs. [16,17,18] for Parts 1, 2 and 3, respectively.