Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model.

@article{Wang2000FreeEC,
  title={Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model.},
  author={Wengang Wang and Peter A. Kollman},
  journal={Journal of molecular biology},
  year={2000},
  volume={303 4},
  pages={567-82}
}
Dimerization of HIV-I protease (HIV PR) monomers is an essential prerequisite for viral proteolytic activity and the subsequent generation of infectious virus particles. Disrupting dimerization of the enzyme can inhibit its activity. We have calculated the relative binding free energies between different dimers of the HIV protease using molecular dynamics and a continuum model, which we call MM/PBSA. We examined the dominant negative inhibition of the HIV PR by a mutated form of the protease… CONTINUE READING

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