Binding memory of liquid molecules

TL;DR

This paper reveals a universal memory effect in the binding dynamics of liquid molecules, combining simulations, theory, and microscopy to understand how environmental factors influence molecular interactions.

Contribution

It introduces a new understanding of binding memory in liquids, integrating multiple methods to quantify and analyze this phenomenon.

Findings

Binding memory exhibits a power-law decay in autocorrelation functions.

Binding memory depends on affinity, topology, and material properties.

Biological systems may exploit this memory to regulate reactions.

Abstract

Understanding the binding dynamics of liquid molecules is of fundamental importance in physical and life sciences. However, nanoscale fast dynamics pose great challenges for experimental characterization. Conventionally, the binding dynamics have been assumed to be memoryless. Here, we integrate large scale computer simulation, scaling theory, and real-time single particle tracking microscopy with high spatiotemporal precision to unveil a universal memory effect in the binding dynamics of liquid molecules. This binding memory can be quantified by a binding time autocorrelation function, whose power-law decay depends not only on the binding affinity, but also on the topological and materials properties of the surrounding environment. Context-dependent biomolecular binding memory is likely exploited by biological systems to regulate biochemical reactions and biophysical processes. Deciphering this binding memory offers a novel strategy to probe complex biological systems and advanced soft materials.