The use of 1JC alpha H alpha coupling constants as a probe for protein backbone conformation.

@article{Vuister1993TheUO,
  title={The use of 1JC alpha H alpha coupling constants as a probe for protein backbone conformation.},
  author={Geerten W. Vuister and Frank Delaglio and Adriaan Bax},
  journal={Journal of biomolecular NMR},
  year={1993},
  volume={3 1},
  pages={67-80}
}
Simple pseudo-3D modifications to the constant-time HSQC and HCACO experiments are described that allow accurate (+/- 0.5 Hz) measurement of one bond JC alpha H alpha coupling constants in proteins that are uniformly enriched with 13C. An empirical phi,psi-surface is calculated which describes the deviation of 1JC alpha H alpha from its random coil value, using 203 1JC alpha H alpha values measured for residues in the proteins calmodulin, staphylococcal nuclease, and basic pancreatic trypsin… CONTINUE READING

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