Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding.
Non-linear rate-equilibrium relationships upon mutation or changes in solvent conditions are frequently observed in protein folding reactions and are usually interpreted in terms of Hammond behavior. Here we first give a general overview over the concept of transition state movements in chemical reactions and discuss its application to protein folding. We then show examples for genuine Hammond behavior and for apparent transition state movements caused by other effects like changes in the rate-limiting step of the folding reaction or ground state effects, i.e. structural changes in either the native state or the unfolded state. These examples show that apparent transition state movements can easily be mistaken for Hammond behavior. We describe experimental tests using self- and cross-interaction parameters to distinguish between structural changes in a single transition state following Hammond behavior and apparent transition state movements caused by other effects.
Sánchez
Ignacio E
IE
Biozentrum der Universität Basel, Department of Biophysical Chemistry, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Kiefhaber
Thomas
T
D004735:Energy Transfer; D007700:Kinetics; D017711:Nonlinear Dynamics; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012997:Solvents
D011506:Proteins; D012997:Solvents