Rigidification of a flexible protease inhibitor variant upon binding to trypsin.

@article{Hanson2007RigidificationOA,
  title={Rigidification of a flexible protease inhibitor variant upon binding to trypsin.},
  author={W. Miachel Hanson and Gretchen J Domek and Martin P. Horvath and David P. Goldenberg},
  journal={Journal of molecular biology},
  year={2007},
  volume={366 1},
  pages={230-43}
}
The Tyr35-->Gly replacement in bovine pancreatic trypsin inhibitor (BPTI) has previously been shown to dramatically enhance the flexibility of the trypsin-binding region of the free inhibitor and to destabilize the interaction with the protease by about 3 kcal/mol. The effects of this replacement on the enzyme-inhibitor interaction were further studied here by X-ray crystallography and isothermal titration calorimetry (ITC). The co-crystal structure of Y35G BPTI bound to trypsin was determined… CONTINUE READING