Thermodynamic relationships between protein-solvent and protein-protein interactions

Lionel Costenaro1, Christine Ebel

  • 1Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale UMR 5075:CEA-CNRS-UJF, 41 rue Jules Horowitz, 38027 Grenoble, France.

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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The formation of a solution is an example of a spontaneous process, which is a process that occurs under specified conditions without energy from some external source.
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The Equilibrium Binding Constant and Binding Strength02:18

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