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={Yasushi Oda and Haruki Nakamura and Toshio Yamazaki and Kuniaki Nagayama and Mayumi Yoshida and Shigenori Kanaya and Morio Ikehara},
  journal={Journal of Biomolecular NMR},
  year={1992},
  volume={2},
  pages={137-147}
}
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… 

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