EXAMINATION OF DYNAMIC PROPERTIES OF BINASE IN SOLUTION BY HYDROGEN-EXCHANGE AND H-1-NMR RELAXATION

The intramolecular mobility of bacterial RNase (binase) in solution wa s studied by hydrogen exchange, nonselective NMR relaxation, and infra red spectroscopy; its secondary structure at pH 1.6-9 was examined. Up on raising the pH from 3.6 to 7, the intensity of intramolecular movem ent decreased, but the secondary structure and local dynamics remained unchanged. This behavior may be attributed to the existence of a hier archy of internal movements affecting the magnetic and chemical relaxa tion parameters.