STUDIES ON HYDRATED LYSOZYME AND ITS THERMAL STABILITY BY NMR
水合溶菌酶及其热稳定性的NMR研究

The proton wide-line NMR spectra and free induction decay curves of hydr- ated lysozyme containing different water content and proton wide-line NMR spectra of hydrated lysozyme(0.10 and 0.19 gH2O/g Lys. respectively)in the temperature range from room temp. to denaturation temp. have been recorded by 90 MHz pulse NMR spectrometer SXP 4-100. The variation of the molecular motions of lysozyme and water in the process of hydration and tnermodcnaturation has been discussed by the changes of line-width parameter with hydration and temperature. The results show that the molecular motions of lysozyme and absorbed water depend on water content and there are two transitions of the molecular motion of lysozyme containing lower water content in the process of thermodenaturation. The two transitions have been considered intermoleculor dissociation and intramolecular unfolding in lysozyme respectively.