Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView.

@article{Schwarzinger2000RandomCC,
  title={Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView.},
  author={Stephan Schwarzinger and Gerard J. A. Kroon and Ted R. Foss and Peter E. Wright and H Jane Dyson},
  journal={Journal of biomolecular NMR},
  year={2000},
  volume={18 1},
  pages={43-8}
}
Studies of proteins unfolded in acid or chemical denaturant can help in unraveling events during the earliest phases of protein folding. In order for meaningful comparisons to be made of residual structure in unfolded states, it is necessary to use random coil chemical shifts that are valid for the experimental system under study. We present a set of random coil chemical shifts obtained for model peptides under experimental conditions used in studies of denatured proteins. This new set… CONTINUE READING

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