Nuclear magnetic resonance studies of the structure and binding sites of enzymes. XI. Characterization of selectively deuterated analogs of staphylococcal nuclease.
The preparation of five different selectively deuterated analogs of the enzyme staphylococcal nuclease has been previously reported.(1-3) The five selectively deuterated enzymes have full enzymatic activity with DNA and RNA substrates and identical amino acid compositions; and they all appear to have similar conformations in solution, despite their very different hydrogen/deuterium contents.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D003851:Deoxyribonucleases / Q000032:analysis*; D003903:Deuterium; D004492:Edetic Acid; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D012260:Ribonucleases / Q000032:analysis*; D012996:Solutions; D013210:Staphylococcus / Q000201:enzymology
D000596:Amino Acids; D012996:Solutions; D004492:Edetic Acid; D003903:Deuterium; D003851:Deoxyribonucleases; D012260:Ribonucleases