Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.

@article{Marassi1997CompleteRO,
  title={Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.},
  author={Francesca M Marassi and Ayyalusamy Ramamoorthy and Stanley J. Opella},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 16},
  pages={8551-6}
}
Complete resolution of the amide resonances in a three-dimensional solid-state NMR correlation spectrum of a uniformly 15N-labeled membrane protein in oriented phospholipid bilayers is demonstrated. The three orientationally dependent frequencies, 1H chemical shift, 1H-15N dipolar coupling, and 15N chemical shift, associated with each amide resonance are responsible for resolution among resonances and provide sufficient angular restrictions for protein structure determination. Because the… CONTINUE READING