Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures.
- 1 January 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (1) , 19-23
- https://doi.org/10.1073/pnas.76.1.19
Abstract
An analysis of the conformational properties of parallel .beta.-pleated sheets suggests that an important factor in the generation of .beta.-sheet twist is the preference for nonplanar peptide bond distortions that impart local left-handed helical character to polypeptide chains. The introduction of such chiral distortions, which result from the tetrahedral deformation of the peptide N atoms, naturally produces right-twisted .beta.-sheet structures with optimal H-bond geometry.This publication has 18 references indexed in Scilit:
- Protein foldingQuarterly Reviews of Biophysics, 1977
- On the conformation of proteins: The handedness of the connection between parallel β-strandsJournal of Molecular Biology, 1977
- Alkylation of a tripeptide by a carcinogen: the crystal structures of sarcosylglycylglycine, 9-methyl-10-chloromethylanthracene, and their reaction productJournal of the American Chemical Society, 1977
- Conformational Analysis of the 20 Naturally Occurring Amino Acid Residues Using ECEPPMacromolecules, 1977
- On the conformation of proteins: The handedness of the β-strand-α-helix-β-strand unitJournal of Molecular Biology, 1976
- Handedness of crossover connections in beta sheets.Proceedings of the National Academy of Sciences, 1976
- The mean geometry of the peptide unit from crystal structure dataBiochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Conformational Analysis of Biopolymers: Conformational Energy CalculationsAnnual Review of Biophysics and Bioengineering, 1972
- Molecular Organization in Alpha-KeratinNature, 1962
- Configurations of Polypeptide Chains With Favored Orientations Around Single BondsProceedings of the National Academy of Sciences, 1951