Thermodynamic and structural effects of conformational constraints in protein-ligand interactions. Entropic paradoxy associated with ligand preorganization.

@article{Delorbe2009ThermodynamicAS,
  title={Thermodynamic and structural effects of conformational constraints in protein-ligand interactions. Entropic paradoxy associated with ligand preorganization.},
  author={John E Delorbe and J. H. Clements and M. Teresk and A. P. Benfield and H. Plake and Laura E Millspaugh and Stephen F Martin},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 46},
  pages={
          16758-70
        }
}
Succinate- and cyclopropane-derived phosphotyrosine (pY) replacements were incorporated into a series of Grb2 SH2 binding ligands wherein the pY+1 residue was varied to determine explicitly how variations in ligand preorganization affect binding energetics and structure. The complexes of these ligands with the Grb2 SH2 domain were examined in a series of thermodynamic and structural investigations using isothermal titration calorimetry and X-ray crystallography. The binding enthalpies for all… Expand
Protein-ligand binding enthalpies from near-millisecond simulations: Analysis of a preorganization paradox.
Thermodynamics of ligand binding and efficiency.
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