Abstract
A heteropolar 2D NMR technique for measurement of {sub 13}C T{sub 1} values in proteins previously reported has been applied to the determination of spin-lattice relaxation times for the {gamma}-carbons of basic pancreatic trypsin inhibitor (BPTI). The technique is described in some detail as applied to BPTI. The lack of dramatic variations noted for T{sub 1} values is taken as assurance that measurements of nuclear Overhauser effects for determination of protein structures in solution are not significantly biased by internal motions, at least as far as the backbone of the protein is concerned. 6 refs., 4 figs.
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