Thermodynamics of Na+ binding to coagulation serine proteases.

@article{Griffon2001ThermodynamicsON,
  title={Thermodynamics of Na+ binding to coagulation serine proteases.},
  author={Nathalie Griffon and Enrico Di Stasio},
  journal={Biophysical chemistry},
  year={2001},
  volume={90 1},
  pages={89-96}
}
The sodium binding to serine proteases triggers a conformational change in the proteins that enhances the catalytic activity of the enzymes. The interaction of the cation with the protein is mediated by the hydrogen-bonding network of water molecules that embed the Na+ site. We pointed out the crucial role of the insertion loop 186a-d and the I16-D194 ion pair in the stabilization of sodium binding pocket in thrombin. This paper contributes to better explain the molecular mechanism of sodium… CONTINUE READING

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