Participation of tryptophan 62 in the self-association of hen egg white lysozyme. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy.
Open Access
- 1 March 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (5), 1795-1798
- https://doi.org/10.1016/s0021-9258(17)40620-x
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- THE DETERMINATION OF THE STRUCTURE OF PROTEINS IN SOLUTION: LYSOZYME *Annals of the New York Academy of Sciences, 1973
- Natural-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Numerous single-carbon resonances of hen egg-white lysozymeBiochemistry, 1973
- Ionization behavior of the catalytic carboxyls of lysozyme. Effects of ionic strengthBiochemistry, 1972
- Effects of pressure and thermodynamic nonideality on the sedimentation equilibrium of chemically reacting systems. Results with lysozyme at pH 6.7 and 8.0The Journal of Physical Chemistry, 1972
- 21 Vertebrate LysozymesPublished by Elsevier ,1972
- Nuclear magnetic resonance study of lysozyme inhibition. Effects of dimerization and pH on saccharide bindingJournal of the American Chemical Society, 1971
- The Lanthanide Cations as Probes in Biological Systems. Proton Relaxation Enhancement Studies for Model Systems and LysozymeEuropean Journal of Biochemistry, 1971
- Self-association of muramidase (lysozyme) in solution at 25°, pH 7.0, and I = 0.20Biochemistry, 1970
- Sedimentation Equilibrium in Reacting Systems. IV. Verification of the Theory*Biochemistry, 1966
- Nuclear Magnetic Resonance Methods for Determining Chemical-Exchange Rates1Journal of the American Chemical Society, 1966