Conformational analysis of poly‐N‐methyl‐L‐alanine
- 1 September 1967
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 5 (9) , 815-820
- https://doi.org/10.1002/bip.1967.360050904
Abstract
Sterically allowed forms of the poly‐N‐methyl‐L‐alanine chain were found by calculation of conformational energies as a function of the rotation angles of its chain bonds. The lowest energy form seems to be a right‐handed, approximately threefold helix.This publication has 8 references indexed in Scilit:
- Conformational Aspects of Polypeptide Structure. XXI. Helical Poly-N-methyl-L-alanine. Theoretical ResultsJournal of the American Chemical Society, 1967
- Stereochemical Code of Amino-Acid Residues: The Molecular Conformation of Gramicidine SNature, 1966
- A proposal of standard conventions and nomenclature for the description of polypeptide conformationsBiopolymers, 1966
- The Configuration of Random Polypeptide Chains. II. TheoryJournal of the American Chemical Society, 1965
- Van Der Waals Interaction and the Stability of Helical Polypeptide ChainsNature, 1965
- Stereochemistry of polypeptide chain configurationsJournal of Molecular Biology, 1963
- Stability of helical conformations of simple linear polymersJournal of Polymer Science Part A: General Papers, 1963
- The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chainProceedings of the National Academy of Sciences, 1951