The α-helix dipole and the properties of proteins
- 1 June 1978
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 273 (5662) , 443-446
- https://doi.org/10.1038/273443a0
Abstract
Phosphate moieties bind frequently at N-termini of helices in proteins. This corresponds with an optimal interaction of the helix dipole and the charged phosphate. This favorable arrangement may have been discovered several times during evolution. In some enzymes, the helix dipole might be used in catalysis.Keywords
This publication has 35 references indexed in Scilit:
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- The peptide chain of tyrosyl tRNA synthetase: No evidence for a super-secondary structure of four α-helicesBiochemical and Biophysical Research Communications, 1977
- Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilusNature, 1977
- Anion binding sites in the active center of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1976
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolutionJournal of Molecular Biology, 1975
- Tertiary structural differences between microbial serine proteases and pancreatic serine enzymesNature, 1975
- Structural and functional similarities within the coenzyme binding domains of dehydrogenasesJournal of Molecular Biology, 1974
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974
- The structure of bovine trypsin : Electron density maps of the inhibited enzyme at 5 Å and at 2·7 Å resolutionJournal of Molecular Biology, 1974
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972