The Glu 2− ⋯ Arg 10+ side-chain interaction in the C-peptide helix of ribonuclease A
Open Access
- 1 August 1990
- journal article
- research article
- Published by Elsevier in Biophysical Chemistry
- Vol. 37 (1-3) , 107-119
- https://doi.org/10.1016/0301-4622(90)88012-h
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- On the fundamental role of the glu 2−…Arg 10+ salt bridge in the folding of isolated ribonuclease a S-peptideBiochemical and Biophysical Research Communications, 1984
- Ion-pairs in proteinsJournal of Molecular Biology, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Helix to helix packing in proteinsJournal of Molecular Biology, 1981
- Effect of low pH on neurophysin-peptide interactions: implications for the stability of the amino-carboxylate salt bridgeBiochemistry, 1977
- Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. IX. Glutamic Acid Parameters from Random Poly(hydroxybutylglutamine-co-L-glutamic acid)Macromolecules, 1975
- The structure of thermolysin: An electron density map at 2.3 Å resolutionJournal of Molecular Biology, 1972
- Polypeptides. XLIV. Potent synthetic S-peptide antagonistsJournal of the American Chemical Society, 1970