Modulation of the affinity of aspartic proteases by the mutated residues in active site models.

@article{Goldblum1990ModulationOT,
  title={Modulation of the affinity of aspartic proteases by the mutated residues in active site models.},
  author={Amiram Goldblum},
  journal={FEBS letters},
  year={1990},
  volume={261 2},
  pages={241-4}
}
The active sites of 3 types of aspartic proteases are modeled, based on crystallographic coordinates of endothiapepsin and of a model of HIV-1 protease. The enthalpies of deprotonation from neutral to mono-anion and to dianion are calculated with semiempirical minimal neglect of differential overlap, hydrogen bonding corrected (MNDO/H). This quantum… CONTINUE READING