By Norman J. Oppenheimer, Thomas L. James
This quantity, as does quantity 176, presents a basic heritage of contemporary NMR options, with a selected specialize in NMR concepts that pertain to proteins and enzymology, and a ''snapshot'' of the present cutting-edge in NMR experimental options. those books allow the reader to appreciate a given approach, to judge its strengths and boundaries, to make your mind up that's the simplest method, and, ultimately, to layout an scan utilizing the selected strategy to clear up an issue
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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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