Chemical compensation in macromolecular bridge-binding to thrombin.

@article{Hopfner1993ChemicalCI,
  title={Chemical compensation in macromolecular bridge-binding to thrombin.},
  author={Karl-Peter Hopfner and Youhna M. Ayala and Zbigniew Szewczuk and Yotaro Konishi and Enrico Di Cera},
  journal={Biochemistry},
  year={1993},
  volume={32 12},
  pages={2947-53}
}
The binding energetics of eight synthetic peptides capable of interfering with thrombin function have been studied by steady-state measurements and clotting assays. The synthetic peptides are bifunctional inhibitors consisting of three domains: (i) a fragment of the C-terminus of recombinant hirudin, hir55-65, which binds to the fibrinogen-recognition site of thrombin; (ii) a small active site inhibitor, Ac-(DF)PRP, binding to the catalytic pocket of the enzyme, and (iii) a linker spanning… CONTINUE READING