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- W1597331152 abstract "The glycosidic bond torsion angles and the conformations of the two riboses of NAD’ bound to yeast and horse liver alcohol dehydrogenase in solution have been determined by a novel method involving the measurement of proton-proton transferred nuclear Overhauser enhancements by ‘H-nuclear magnetic resonance. In both cases the conformation of the-a8eirosine and nicotinamide ribose is 3’-endo of the N type. The conformations about both glycosidic bonds are anti with xA (0-4’-C-l’-N-9-C-4) - 270” and 240” for yeast and horse liver alcohol dehydrogenase, respectively, and xN (O-4’-C-l’-N-1-C-2) - 240” for both yeast and horse liver alcohol dehydrogenase." @default.
- W1597331152 created "2016-06-24" @default.
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- W1597331152 date "1982-01-01" @default.
- W1597331152 modified "2023-09-27" @default.
- W1597331152 title "Conformation of NAD+ Bound to Yeast and Horse Liver Alcohol Dehydrogenase in Solution" @default.
- W1597331152 hasPublicationYear "1982" @default.
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