Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface.

@article{Loladze1999EngineeringAT,
  title={Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface.},
  author={Vakhtang V Loladze and Beatriz Ibarra-Molero and Jose M. Sanchez-Ruiz and George I. Makhatadze},
  journal={Biochemistry},
  year={1999},
  volume={38 50},
  pages={16419-23}
}
A simple theoretical model for increasing the protein stability by adequately redesigning the distribution of charged residues on the surface of the native protein was tested experimentally. Using the molecule of ubiquitin as a model system, we predicted possible amino acid substitutions on the surface of this protein which would lead to an increase in its stability. Experimental validation for this prediction was achieved by measuring the stabilities of single-site-substituted ubiquitin… CONTINUE READING