Enzyme-inhibitor association thermodynamics: explicit and continuum solvent studies.

@article{Resat1997EnzymeinhibitorAT,
  title={Enzyme-inhibitor association thermodynamics: explicit and continuum solvent studies.},
  author={Haluk Resat and Tami Marrone and J. Andrew McCammon},
  journal={Biophysical journal},
  year={1997},
  volume={72 2 Pt 1},
  pages={522-32}
}
Studying the thermodynamics of biochemical association reactions at the microscopic level requires efficient sampling of the configurations of the reactants and solvent as a function of the reaction pathways. In most cases, the associating ligand and receptor have complementary interlocking shapes. Upon association, loosely connected or disconnected solvent cavities at and around the binding site are formed. Disconnected solvent regions lead to severe statistical sampling problems when… CONTINUE READING

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