By G. S. Voronov
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2] D e u t e r a t i o n in P r o t e i n P r o t o n M a g n e t i c R e s o n a n c e B y DAVID M. LEMASTER Deuteration techniques in protein NMR serve as a means of modifying ~H spectra for improved resolution and assignment purposes as well as providing increased sensitivity for direct 2H observation (see Keniry [19], Vol. 176, this series). There are three general patterns of deuterium labeling that in practice serve rather different functions: selective protonation in a deutero background, selective deuteration in a protio background, and random fractional deuteration in which all carbon-bound hydrogen positions have been uniformly enriched to an intermediate level with deuterium.
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