Changes in residual protein entropy are a potentially important component of the change in the free energy of protein association, but such thermodynamics have been virtually impossible to determine experimentally. Here the authors used solution NMR spectroscopy to show that the change in internal dynamics of calmodulin varies significantly on binding a variety of target domains, which indicates that changes in residual protein conformational entropy can contribute significantly to the free energy of protein-ligand association.
- Kendra King Frederick
- Michael S. Marlow
- A. Joshua Wand
