Hydrogen exchange in unligated and ligated staphylococcal nuclease.

@article{Loh1993HydrogenEI,
  title={Hydrogen exchange in unligated and ligated staphylococcal nuclease.},
  author={Stewart N. Loh and Kenneth E Prehoda and Jian Wang and John L. Markley},
  journal={Biochemistry},
  year={1993},
  volume={32 41},
  pages={11022-8}
}
The exchange kinetics of over 70% of the 143 backbone amide hydrogens in staphylococcal nuclease H124L (nuclease H124L), both in its unligated state and in its ternary complex with Ca2+ and thymidine 3',5'-bisphosphate, have been quantified by nitrogen-15 resolved proton nuclear magnetic resonance spectroscopy. Protection factors for the slowly exchanging hydrogens in unligated nuclease H124L at 37 degrees C and pH 5.5 were found to vary by over one order of magnitude. This range of protection… CONTINUE READING

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The exchange kinetics of over 70% of the 143 backbone amide hydrogens in staphylococcal nuclease H124L ( nuclease H124L ) , both in its unligated state and in its ternary complex with Ca2 + and thymidine 3',5'-bisphosphate , have been quantified by nitrogen-15 resolved proton nuclear magnetic resonance spectroscopy .
The exchange kinetics of over 70% of the 143 backbone amide hydrogens in staphylococcal nuclease H124L ( nuclease H124L ) , both in its unligated state and in its ternary complex with Ca2 + and thymidine 3',5'-bisphosphate , have been quantified by nitrogen-15 resolved proton nuclear magnetic resonance spectroscopy .
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