Theoretical Structure Investigations of N-Acetyl-L-Proline Amide

by Ramek, M.; Kelterer, A. M.; Teppen, B. J.; Schafer, L.

The potential energy surface of N-acetyl-L-proline amide has been investigated via RHF, AM1, and PM3 calculations. The results show significant differences between these methods: seven local minima can be found with RHF, three with AM1, 17 with PM3. The conformation of the RHF/6-31G* global minimum corresponds to the gamma-turn structure of polypeptides. In contrast to this, the proline conformer that participates in the formation of ten-membered beta-turns in peptide chains has a relatively high energy in the dipeptide.

Journal
Journal of Molecular Structure
Volume
352
Year
1995
Start Page
59-70
URL
https://dx.doi.org/10.1016/0022-2860(94)08499-8
ISBN/ISSN
1872-8014; 0022-2860
DOI
10.1016/0022-2860(94)08499-8