Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein.

@article{LindorffLarsen2004DeterminationOA,
  title={Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein.},
  author={Kresten Lindorff-Larsen and Sigridur Soley Kristjansdottir and Kaare Teilum and Wolfgang Fieber and Christopher M. Dobson and Flemming M. Poulsen and Michele Vendruscolo},
  journal={Journal of the American Chemical Society},
  year={2004},
  volume={126 10},
  pages={
          3291-9
        }
}
The denatured state of a protein contains important information about the determinants of the folding process. By combining site-directed spin-labeling NMR experiments and restrained computer simulations, we have determined ensembles of conformations that represent the denatured state of the bovine acyl-coenzyme A binding protein (ACBP) at three different concentrations of guanidine hydrochloride. As the experimentally determined distance information corresponds to weighted averages over a… CONTINUE READING

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