Water interactions with varying molecular states of bovine casein: 2H NMR relaxation studies
- 1 September 1987
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 257 (2) , 259-268
- https://doi.org/10.1016/0003-9861(87)90565-0
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Nomenclature of Proteins of Cow's Milk: Fifth RevisionJournal of Dairy Science, 1984
- Interactions Leading to Formation of Casein SubmicellesJournal of Dairy Science, 1982
- A deuteron and proton magnetic resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteinsArchives of Biochemistry and Biophysics, 1982
- Molecular Interactions in β-Lactoglobulin. X. The Stoichiometry of the β-Lactoglobulin Mixed Tetramerization1Journal of the American Chemical Society, 1966
- Molecular Interactions in β-Lactoglobulin. VIII. Small-Angle X-Ray Scattering Investigation of the Geometry of β-Lactoglobulin A TetramerizationJournal of the American Chemical Society, 1964
- Molecular Interactions in β-Lactoglobulin. V. the Association of the Genetic Species of β-Lactoglobulin below the Isoelectric Point2Journal of the American Chemical Society, 1961
- Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22Journal of the American Chemical Society, 1960
- Molecular Interactions in β-Lactoglobulin. II. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin below its Isoelectric Point2Journal of the American Chemical Society, 1960
- Relaxation Processes in a System of Two SpinsPhysical Review B, 1955
- A General Theory of Magnetic Resonance AbsorptionJournal of the Physics Society Japan, 1954