The structure of unnatural hexapeptides, containing three L-valine units and three unnatural a amino acids ((2R)-methyl aspartic acid, (2S)-methylornitine and modified proline), has been elucidated using 1H NMR and IR spectroscopy and a 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.
M. Calvaresi, D. Balducci, A. Bottoni, G. Porzi (2009). Conformational Analysis of Hexapseudopeptides Mimicking Reverse Turn Structures Induced by a Modified (S)-Proline. A Combined Spectroscopic and Molecular Dynamics Investigation. Part 4. MOLECULAR PHYSICS, 107, 653-663 [10.1080/00268970902845339].
Conformational Analysis of Hexapseudopeptides Mimicking Reverse Turn Structures Induced by a Modified (S)-Proline. A Combined Spectroscopic and Molecular Dynamics Investigation. Part 4
CALVARESI, MATTEO;BALDUCCI, DANIELE;BOTTONI, ANDREA;PORZI, GIANNI
2009
Abstract
The structure of unnatural hexapeptides, containing three L-valine units and three unnatural a amino acids ((2R)-methyl aspartic acid, (2S)-methylornitine and modified proline), has been elucidated using 1H NMR and IR spectroscopy and a 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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
