1H-NMR relaxation studies of native and thermally denatured lysozyme solutions: an isotope dilution experiment.
1H-NMR relaxation times are reported for native and thermally denatured lysozyme aqueous solutions measured as the function of the proton mole fraction in the sample. A two-exponential character of proton longitudinal relaxation function was observed for native lysozyme solutions: the fast component was attributed to the non-exchangeable protein protons, the slow one to water protons. Purely exponential decay of longitudinal magnetization was observed for the thermally denatured samples. This has been explained in terms of a fast spin exchange model. The contributions of the protein protons to the water proton relaxation rate in native and thermally denatured samples were determined, too.
D000818:Animals; D002645:Chickens; D005260:Female; D006358:Hot Temperature; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase; D010063:Ovum / Q000201:enzymology; D011489:Protein Denaturation
D009113:Muramidase