Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.

@article{Pace2000ChargechargeII,
  title={Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.},
  author={C. Nick Pace and Roy W Alston and Kevin L Shaw},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 7},
  pages={1395-8}
}
Several recent studies have shown that it is possible to increase protein stability by improving electrostatic interactions among charged groups on the surface of the folded protein. However, the stability increases are considerably smaller than predicted by a simple Coulomb's law calculation, and in some cases, a charge reversal on the surface leads to a decrease in stability when an increase was predicted. These results suggest that favorable charge-charge interactions are important in… CONTINUE READING