Protein folding intermediates and pathways studied by hydrogen exchange.

@article{Englander2000ProteinFI,
  title={Protein folding intermediates and pathways studied by hydrogen exchange.},
  author={S. Walter Englander},
  journal={Annual review of biophysics and biomolecular structure},
  year={2000},
  volume={29},
  pages={213-38}
}
In order to solve the immensely difficult protein-folding problem, it will be necessary to characterize the barriers that slow folding and the intermediate structures that promote it. Although protein-folding intermediates are not accessible to the usual structural studies, hydrogen exchange (HX) methods have been able to detect and characterize intermediates in both kinetic and equilibrium modes--as transient kinetic folding intermediates on a subsecond time scale, as labile equilibrium molten… CONTINUE READING

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Structural characterization of folding intermediates in cytochrome c by Hexchange labeling and proton NMR

  • H Roder, GA El ̈ ove, SW. Englander
  • 1988
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