Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.

@article{Chen2000IncreasingTT,
  title={Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.},
  author={Junmei Chen and Zhiqiang Lu and Joshua Sakon and Wesley E. Stites},
  journal={Journal of molecular biology},
  year={2000},
  volume={303 2},
  pages={125-30}
}
Seven hyper-stable multiple mutants have been constructed in staphylococcal nuclease by various combinations of eight different stabilizing single mutants. The stabilities of these multiple mutants determined by guanidine hydrochloride denaturation were 3.4 to 5.6 kcal/mol higher than that of the wild-type. Their thermal denaturation midpoint temperatures were 12.6 to 22.9 deg. C higher than that of the wild-type. These are among the greatest increases in protein stability and thermal… CONTINUE READING