The idea that entropic effects play a major role in enzyme catalysis has been invoked frequently.
In order to quantify this possibility we developed a restraint release (RR) approach for the evaluation of activation entropies in enzymes and solution reactions1,2
The RR approach appears to be a particularly powerful strategy overcoming the major problems of most current approach, including the inherent unreliability of quasi harmonic and related approaches.
Our initial studies indicated that the entropic contributions to catalysis are much less important than previously thought.
We have continued in exploring entropic effects to binding3
using the RR approach will also explored entropic contributions to enantioselectivity6
We continue to push the frontiers in developing and using efficient and reliable ways for calculations entropy in proteins.
Thermodynamic cycle for the evaluation of the RR configurational entropy contribution to the activation free energy for the RS and the TS, states I and II respectively.