Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide.

@article{Chang2000StructureAH,
  title={Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide.},
  author={J Y Chang and A M Ballatore},
  journal={Journal of protein chemistry},
  year={2000},
  volume={19 4},
  pages={299-310}
}
Tick anticoagulant peptide (TAP) is a factor Xa-specific inhibitor and is structurally homologous to bovine pancreatic trypsin inhibitor (BPTI). The fully reduced TAP refolds spontaneously to form the native structure under a wide variation of redox buffers. The folding intermediates of TAP consist of at least 22 fractions of one-disulfide, two-disulfide, and three-disulfide scrambled isomers. Three species of well-populated one- and two-disulfide intermediates were isolated and structurally… CONTINUE READING