# Minimum energy paths for conformational changes of viral capsids

## TL;DR

This paper applies Large Deviations Theory to model the conformational changes of a viral capsid, identifying the most probable transition paths and analyzing the stability of intermediate states in a simplified dodecahedral model.

## Contribution

It introduces a novel application of Large Deviations Theory to study energy paths in viral capsid conformational changes, focusing on a simplified geometric model.

## Key findings

- Computed minimum energy paths for capsid transition
- Identified stable intermediate states during conformational change
- Provided insights into the stability of weakly interacting protein structures

## Abstract

In this work we study how a viral capsid can change conformation using techniques of Large Deviations Theory for stochastic differential equations. The viral capsid is a model of a complex system in which many units - the proteins forming the capsomers - interact by weak forces to form a structure with exceptional mechanical resistance. The destabilization of such a structure is interesting both per se, since it is related either to infection or maturation processes, and because it yields insights into the stability of complex structures in which the constitutive elements interact by weak attractive forces. We focus here on a simplified model of a dodecahederal viral capsid, and assume that the capsomers are rigid plaquettes with one degree of freedom each. We compute the most probable transition path from the closed capsid to the final configuration using minimum energy paths, and discuss the stability of intermediate states.