Internal dynamics of human ubiquitin revealed by 13C-relaxation studies of randomly fractionally labeled protein.

@article{Wand1996InternalDO,
  title={Internal dynamics of human ubiquitin revealed by 13C-relaxation studies of randomly fractionally labeled protein.},
  author={A Joshua Wand and Jeffrey L. Urbauer and Richard P. McEvoy and R J Bieber},
  journal={Biochemistry},
  year={1996},
  volume={35 19},
  pages={6116-25}
}
The use of random, fractional 13C-enrichment combined with low pass filtration has allowed the determination of NMR relaxation parameters at an unprecedented number of sites within recombinant human ubiquitin. Essentially complete 1H, 13C, and 15N resonance assignments for the protein are reported. Carbon spin lattice and heteronuclear NOE relaxation data have been analyzed in the context of the Lipari-Szabo "model free" formalism. The generalized order parameters for 56 main chain alpha C-H… CONTINUE READING

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