Structure of proteins: packing of alpha-helices and pleated sheets.
Open Access
- 1 October 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (10), 4130-4134
- https://doi.org/10.1073/pnas.74.10.4130
Abstract
Simple models are presented that describe the rules for almost all the packing that occurs between and among alpha-helices and pleated sheets. These packing rules, together with the primary and secondary structures, are the major determinants of the three-dimensional structure of proteins.This publication has 9 references indexed in Scilit:
- Thermodynamic fluctuations in protein molecules.Proceedings of the National Academy of Sciences, 1976
- Structural patterns in globular proteinsNature, 1976
- Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor.Proceedings of the National Academy of Sciences, 1975
- Alpha-carbon coordinates for bovine Cu, Zn superoxide dismutaseBiochemical and Biophysical Research Communications, 1975
- Structural invariants in protein foldingNature, 1975
- The interpretation of protein structures: Total volume, group volume distributions and packing densityJournal of Molecular Biology, 1974
- Conformation of twisted β-pleated sheets in proteinsJournal of Molecular Biology, 1973
- The Polypeptide-Chain Configuration in Hbmoglobin and Other Globular ProteinsProceedings of the National Academy of Sciences, 1951
- The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chainProceedings of the National Academy of Sciences, 1951