Abstract
Broad-line proton magnetic resonance (PMR) and differential thermal analysis (DTA) were employed to investigate the molecular motion of crystalline lysozyme. The motional narrowing of the broad component of PMR and the endothermal peak in DTA were observed at almost the same temperature. This temperature changed reversibly from about 70 to 200°C depending upon the water content of the sample. The PMR line-narrowing and the endothermal peaks are thought to be due to the conformational changes of the protein caused by the melting of the crystals. By applying Flory’s theory of the melting point depression, it was shown that the interaction energy between water and lysozyme molecule became larger in a region where the water content was below 15 wt%. Furthermore, PMR line-narrowing of narrow component was observed in the temperature range from 20 to 50°C. The corresponding small endothermal peak was also observed in DTA.
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