Early events in the disulfide-coupled folding of BPTI.

@article{Bulaj1999EarlyEI,
  title={Early events in the disulfide-coupled folding of BPTI.},
  author={Grzegorz Bulaj and David P. Goldenberg},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 9},
  pages={1825-42}
}
Recent studies of the refolding of reduced bovine pancreatic trypsin inhibitor (BPTI) have shown that a previously unidentified intermediate with a single disulfide is formed much more rapidly than any other one-disulfide species. This intermediate contains a disulfide that is present in the native protein (between Cys14 and 38), but it is thermodynamically less stable than the other two intermediates with single native disulfides. To characterize the role of the [14-38] intermediate and the… CONTINUE READING
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