Summary
1. Spatial forms of Ac-L-Ala-L-Pro-L-Ala-NHMe with trans peptide bonds are the most preferred. Elongation of the peptide chain promotes the stabilization of the trans configuration of the tertiary amide group.
2. In the structure of the compound investigated, the dominating role is played by the interaction of the neighboring residues.
3. Of the six types of conformations of X-Pro-Y observed in proteins, the first four belong to the preferred forms of the Ac-L-Ala-L-Pro-L-Ala-NHMe molecule.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature cited
V. Z. Pletnev, É. P. Gromov, and D. M. Popov, Khim. Prirodn. Soedin., No. 5, p. 618 (1975).
E. M. Popov, G. M. Lipkind, S. F. Arkhipova, and V. G. Dashevskii, Molekul. Biol.,3, 622 (1968).
Additional information
M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Science of the USSR. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 626–630, September–October, 1975.
Rights and permissions
About this article
Cite this article
Gromov, É.P., Pletnev, V.Z. & Popov, E.M. Theoretical conformational analysis of the methylamide of N-acetyl-L-alanyl-L-prolyl-L-alanine. II. Chem Nat Compd 11, 655–659 (1975). https://doi.org/10.1007/BF00567706
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF00567706