Experimental measurement of binding energy, selectivity and allostery using fluctuation theorems

Abstract

Thermodynamic bulk measurements of binding reactions critically rely on the validity of the law of mass action and the assumption of a dilute solution. Yet important biological systems such as allosteric ligand-receptor binding, macromolecular crowding, or misfolded molecules may not follow this fundamental law and require a particular reaction model. Here we introduce a fluctuation theorem for ligand binding and an experimental approach using single-molecule force-spectroscopy to determine binding energies, selectivity and allostery of nucleic acids, proteins and peptides in a model-independent fashion. This work extends the use of fluctuation theorems beyond unimolecular folding reactions, bridging the thermodynamics of small systems and the basic laws of chemical equilibrium.

References in corpus (4)

• Single-molecule derivation of salt dependent base-pair free energies in DNA
• Experimental free energy measurements of kinetic molecular states using fluctuation theorems
• Improving signal-to-noise resolution in single molecule experiments using molecular constructs with short handles
• Recovery of free energy branches in single molecule experiments

Cited by in corpus (5)

• Large work extraction and the Landauer limit in a continuous Maxwell demon
• Stem-loop formation drives RNA folding in mechanical unzipping experiments
• Efficient methods for determining folding free energies in single-molecule pulling experiments
• Dissipation reduction and information-to-measurement conversion in DNA pulling experiments with feedback protocols
• White-noise fluctuation theorem for Langevin dynamics