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Hydrodynamic steering effects in protein association

D Brune¹, S Kim

¹Department of Chemical Engineering, University of Wisconsin, Madison 53705.

Proceedings of the National Academy of Sciences of the United States of America

|April 12, 1994

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Hydrodynamic forces, specifically steering torques, significantly enhance protein-ligand reaction rates by aiding orientation. These effects can be much stronger than electrostatic interactions.

Area of Science:

Biochemistry and Biophysics
Chemical Kinetics
Molecular Dynamics

Background:

Protein-ligand reaction rates are frequently limited by diffusion and the requirement for precise molecular orientation.
Existing models often overlook non-electrostatic forces influencing molecular encounters in solution.

Purpose of the Study:

To investigate the role of hydrodynamic forces in enhancing protein-ligand reaction rates.
To quantify the contribution of hydrodynamic steering torques compared to electrostatic interactions.

Main Methods:

Utilized cleft enzymes as a model system to study hydrodynamic effects.
Developed a simple model to compare hydrodynamic steering torques with electrostatic torques between protein-sized dipoles.

Main Results:

Related Experiment Videos

Identified a significant steering torque arising from the movement of water molecules during protein-ligand encounter.
Demonstrated that hydrodynamic steering torques can be up to two orders of magnitude greater than electrostatic torques.

Conclusions:

Hydrodynamic interactions, particularly steering torques, play a crucial role in overcoming orientation limitations for protein-ligand reactions.
These findings suggest that hydrodynamic forces are a major determinant of reaction rates in solution, potentially explaining faster-than-expected kinetics.