DENATURATION OF PROTEINS. V.* N.M.R. STUDY OF THE ARGININE RESIDUES OF LYSOZYME
- 12 January 2009
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 6 (5) , 295-302
- https://doi.org/10.1111/j.1399-3011.1974.tb02388.x
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Determination of the Dissociation Constants of the Lysine Residues of Lysozyme by Proton‐Magnetic‐Resonance SpectroscopyEuropean Journal of Biochemistry, 1973
- Study of the chemical denaturation of lysozyme by optical mixing spectroscopyBiochemistry, 1973
- NMR Studies of the unfolding of ribonuclease by guanidine hydrochloride. Evidence for intermediate statesFEBS Letters, 1973
- Kinetics of unfolding and refolding of proteinsJournal of Molecular Biology, 1973
- Kinetics of unfolding and refolding of proteinsJournal of Molecular Biology, 1973
- A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease AJournal of Molecular Biology, 1972
- Optical Rotatory Dispersion and Nuclear Magnetic Resonance. Studies of Helix Coil Transitions in Poly-l-Arginine, Poly-l-Lysine and HistonesEuropean Journal of Biochemistry, 1970
- Nuclear magnetic resonance spectroscopy of denatured proteinsAustralian Journal of Chemistry, 1969
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967
- Equilibrium and kinetics of the unfolding of lysozyme (muramidase) by guanidine hydrochlorideJournal of Molecular Biology, 1966