Dry and wet interfaces: Influence of solvent particles on molecular recognition

TL;DR

This study uses a coarse-grained lattice model to explore how water molecules at protein interfaces influence molecular recognition, revealing that optimal water content can enhance selectivity depending on interface hydrophobicity.

Contribution

The paper introduces a model incorporating explicit solvent effects to analyze how water influences protein recognition selectivity, highlighting the importance of dry versus wet interfaces.

Findings

Optimal water fraction maximizes recognition selectivity.

Selectivity depends on interface hydrophobicity.

Water presence can be tuned to improve recognition performance.

Abstract

We present a coarse-grained lattice model to study the influence of water on the recognition process of two rigid proteins. The basic model is formulated in terms of the hydrophobic effect. We then investigate several modifications of our basic model showing that the selectivity of the recognition process can be enhanced by considering the explicit influence of single solvent particles. When the number of cavities at the interface of a protein-protein complex is fixed as an intrinsic geometric constraint, there typically exists a characteristic fraction that should be filled with water molecules such that the selectivity exhibits a maximum. In addition the optimum fraction depends on the hydrophobicity of the interface so that one has to distinguish between dry and wet interfaces.