NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states.

@article{Nkari2009NMRRA,
  title={NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states.},
  author={Wendy K Nkari and James H. Prestegard},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 14},
  pages={5344-9}
}
Protein NMR assignments of large proteins using traditional triple resonance techniques depends on double or triple labeling of samples with (15)N, (13)C, and (2)H. This is not always practical with proteins that require expression in nonbacterial hosts. Labeling with isotopically labeled versions of single amino acids (sparse labeling) often is possible; however, resonance assignment then requires a new strategy. Here a procedure for the assignment of cross-peaks in (15)N-(1)H correlation… CONTINUE READING