Protein folding monitored at individual residues during a two-dimensional NMR experiment.

@article{Balbach1996ProteinFM,
  title={Protein folding monitored at individual residues during a two-dimensional NMR experiment.},
  author={Jochen Balbach and Vincent Forge and W. S. Lau and Nico A J van Nuland and Keith Brew and Christopher M. Dobson},
  journal={Science},
  year={1996},
  volume={274 5290},
  pages={1161-3}
}
An approach is described to monitor directly at the level of individual residues the formation of structure during protein folding. A two-dimensional heteronuclear nuclear magnetic resonance (NMR) spectrum was recorded after the rapid initiation of the refolding of a protein labeled with nitrogen-15. The intensities and line shapes of the cross peaks in the spectrum reflected the kinetic time course of the folding events that occurred during the spectral accumulation. The method was used to… CONTINUE READING

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