# Stimulated binding of polymer chains by narrow tube confinement

## TL;DR

This paper investigates how narrow tube confinement induces binding between unfolded protein chains by reducing their entropy, using simulations to identify the critical conditions and length scales for such binding.

## Contribution

It introduces a novel understanding of polymer chain binding under severe confinement, highlighting entropy-driven interactions in biological channels.

## Key findings

- Binding propensity increases with confinement
- Critical tube diameter for binding identified
- Average binding length m* quantified

## Abstract

In biology, there are several processes in which unfolded protein chains are transported along narrow-tube channels. Normally, without such a severe configurational constraint, unfolded polypeptides would not bind to each other. However, when chain entropy is much reduced in the narrow channel, we find that polypeptide chains have a propensity to bind, even if there is no great potential energy gain in doing so. We find the average length of binding m* (the number of monomers at the chain ends that form bonds) and the critical tube diameter at which such constrained binding occurs. We carry out Brownian dynamics simulations of tightly confined chains, demonstrating their binding over the characteristic length m*, changing in tubes of different diameter.