1H NMR studies of deuterated ribonuclease HI selectively labeled with protonated amino acids

@article{Oda19921HNS,
  title={1H NMR studies of deuterated ribonuclease HI selectively labeled with protonated amino acids},
  author={Y. Oda and H. Nakamura and T. Yamazaki and K. Nagayama and M. Yoshida and S. Kanaya and M. Ikehara},
  journal={Journal of Biomolecular NMR},
  year={1992},
  volume={2},
  pages={137-147}
}
  • Y. Oda, H. Nakamura, +4 authors M. Ikehara
  • Published 1992
  • Chemistry, Medicine
  • Journal of Biomolecular NMR
  • SummaryTwo-dimensional (2D)1H NMR experiments using deuterium labeling have been carried out to investigate the solution structure of ribonuclease HI (RNase HI) fromEscherichia coli (E. coli), which consists of 155 amino acids. To simplify the1H NMR spectra, two fully deuterated enzymes bearing several prototed amino acids were prepared from an RNase HI overproducing strain ofE. coli grown in an almost fully deuterated medium. One enzyme was selectively labeled by protonated His, He. Val. and… CONTINUE READING
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    References

    SHOWING 1-10 OF 24 REFERENCES
    NMR of proteins and nucleic acids
    • 6,828
    • PDF
    NMR studies of a complex of deuterated calmodulin with melittin.
    • 64
    • PDF