Structure and conformation of linear peptides
- 1 July 1984
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 24 (1) , 55-59
- https://doi.org/10.1111/j.1399-3011.1984.tb00927.x
Abstract
The crystal structure of L-tyrosyl-L-tyrosine was determined. The molecule exists as a zwitterion, the peptide unit is trans planar, and the backbone torsion angles correspond to an extended conformation, with .psi.1 = 149.4.degree., .vphi.2 = -161.2.degree., .psi.2 = 158.3.degree.. The values of the side-chain torsion angles (.chi.1, .chi.2) are (-58.8.degree., -63.1.degree.) for the first tyrosine (-171.7.degree., -116.5.degree.) for the second. The planes of the aromatic rings are nearly parallel (dihedral angle of 6.1.degree.), and their centers are separated by 10.9 .ANG.. The carboxyl plane forms a dihedral angle of 23.8.degree. with the plane of the peptide bond.Keywords
This publication has 5 references indexed in Scilit:
- Structure du chlorure de L-tyrosyl-L-phénylalanineActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1982
- The crystal structure of pepsin substrate: N-acetyl-L-phenyl-alanyl-L-tyrosineActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1973
- IUPAC-IUB Commission on Biochemical Nomenclature. Abbreviations and symbols for the description of the conformation of polypeptide chains. Tentative rules (1969)Biochemistry, 1970
- Coherent X-Ray Scattering for the Hydrogen Atom in the Hydrogen MoleculeThe Journal of Chemical Physics, 1965
- The Crystal Structure of MelamineJournal of the American Chemical Society, 1941