# Entropy facilitated active transport

## TL;DR

This paper proposes an entropy-based interpretation of active ion transport, linking pore geometry to driving force and Gibbs energy changes, with significant entropic contributions observed in various proteins.

## Contribution

It introduces a novel entropy-facilitated perspective on active transport, connecting pore geometry to thermodynamic driving forces.

## Key findings

- Entropic contribution from pore geometry is significant in several proteins.
- Pore geometry influences the Gibbs energy and affinity variations.
- The approach offers a new way to interpret active transport mechanisms.

## Abstract

We show how active transport of ions can be interpreted as an entropy facilitated process. In this interpretation, the pore geometry through which substrates are transported can give rise to a driving force. This gives a direct link between the geometry and the changes in Gibbs energy required. Quantifying the size of this effect for several proteins we find that the entropic contribution from the pore geometry is significant and we discuss how the effect can be used to interpret variations in the affinity at the binding site.