Crystallographic and kinetic evidence of allostery in a trypsin-like protease.

@article{Niu2011CrystallographicAK,
  title={Crystallographic and kinetic evidence of allostery in a trypsin-like protease.},
  author={Weiling Niu and Zhiwei Chen and P. S. Sudhakar Gandhi and Austin D. Vogt and Nicola Pozzi and Leslie A. Pelc and Fatima Zapata and Enrico Di Cera},
  journal={Biochemistry},
  year={2011},
  volume={50 29},
  pages={
          6301-7
        }
}
Protein allostery is based on the existence of multiple conformations in equilibrium linked to distinct functional properties. Although evidence of allosteric transitions is relatively easy to identify by functional studies, structural detection of a pre-existing equilibrium between alternative conformations remains challenging even for textbook examples of allosteric proteins. Kinetic studies show that the trypsin-like protease thrombin exists in equilibrium between two conformations where the… CONTINUE READING
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