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Conformational analysis of hexapseudopeptides mimicking reverse turn structures induced by a modified (S)-proline. A combined spectroscopic and molecular dynamics investigation. Part 4

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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.
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Keywords: NMR spectroscopy; cluster analysis; conformational analysis; molecular dynamics; unnatural hexapeptides

Document Type: Research Article

Affiliations: Dipartimento di Chimica 'G. Ciamician', Universita di Bologna, 40126 Bologna, Italy

Publication date: 2009-10-01

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