Proton magnetic resonance study of Crambin, a hyperstable hydrophobic protein, at 250 and 600 MHz
- 18 March 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (6), 1140-1145
- https://doi.org/10.1021/bi00547a016
Abstract
No abstract availableKeywords
This publication has 3 references indexed in Scilit:
- Highly ordered crystals of the plant seed protein crambinJournal of Molecular Biology, 1979
- Proton magnetic resonance spectra at 220 MHz of amino acids, porcine and bovine insulin and the A and B chains of bovine insulinJournal of Molecular Spectroscopy, 1968
- Slow Tritium-Hydrogen Exchange in Some Cyclic Peptide Chelates*Biochemistry, 1967