Theoretical structure investigations of N-acetyl-l-proline amide

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...

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Bibliographic Details
Published in:Journal of molecular structure 1995, Vol.352, p.59-70
Main Authors: Ramek, Michael, Kelterer, Anne-Marie, Teppen, Brian J., Schäfer, Lothar
Format: Article
Language:English
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Summary: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 γ-turn structure of polypeptides. In contrast to this, the proline conformer that participates in the formation of ten-membered β-turns in peptide chains has a relatively high energy in the dipeptide.
ISSN:0022-2860
1872-8014
DOI:10.1016/0022-2860(94)08499-8