Abstract
Tritium NMR spectroscopy of specifically tritiated and tritiated/deuterated derivatives of tosylchymotrypsin has been used to examine the properties of the tosyl group in this protein. The presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of the composite relaxation behavior of the collection of tritiated species present were used in conjunction with models developed from crystallographic results to interpret the observations made. These analyses suggest that the tosyl group of tosylchymotrypsin at pH 4 is highly mobile in solution and, on average, only occupies the location in the protein that is observed in the solid state about 50% of the time. 31 refs., 5 figs., 1 tab.
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