A single protein-ligand complex is the result of a complicated mixture of attractive and repulsive intermolecular interactions that together lead to favorable binding and a negative binding free energy (-△G). The associated enthalpy and entropy terms that make up a -△G, and their compensatory relationship, have been notoriously difficult to deconvolute especially for weakly-bound multi-component interactions.<br/>We are interested in finding new, experimental methods that can accurately account for the enthalpic and entropic components that drive noncovalent binding. The test system we employ is a molecular torsion balance, which can probe the residual entropy that resides in weakly-bound states. Our experimental design, synthesis, and efforts toward quantifying entropic and enthalpic contributions in solution-phase binding will be presented.

Exploring the hidden role of entropy in noncovalent interactions: Molecular torsion balance approach

ACS Spring 2022

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