Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis.

@article{Leung2001SignificanceOL,
  title={Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis.},
  author={K. W.-S. Leung and Y-C. Liaw and Siu Chiu Chan and Ho Yin Lo and Faik N. Musayev and Jun Chen and Hongbo Fang and Hueih Min Chen},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 49},
  pages={46039-45}
}
In this paper, we show that amino acids Glu(73) and Asp(77) of staphylococcal nuclease cooperate unequally with Glu(75) to stabilize its structure located between the C-terminal helix and beta-barrel of the protein. Amino acid substitutions E73G and D77G cause losses of the catalytic efficiency of 24 and 16% and cause thermal stability losses of 22 and 26%, respectively, in comparison with the wild type (WT) protein. However, these changes do not significantly change global and local secondary… CONTINUE READING