Free energy landscapes of encounter complexes in protein-protein association

From: Biophysical Journal | Date: March 1, 1999| Author: | Copyright information

ABSTRACT We report the computer generation of a high-density map of the thermodynamic properties of the diffusionaccessible encounter conformations of four receptor-ligand protein pairs, and use it to study the electrostatic and desolvation components of the free energy of association. Encounter complex conformations are generated by sampling the translational/ rotational space of the ligand around the receptor, both at 5-Angstrom and zero surface-to-surface separations. We find that partial desolvation is always an important effect, and it becomes dominant for complexes in which one of the ...

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