# Partition Function Zeros and Heat Capacity Decomposition Reveal HP Protein Foldability

## TL;DR

This paper shows how a thermodynamic method can be used to evaluate how well proteins fold based on their heat capacity and transition behavior.

## Contribution

The extension of heat capacity decomposition using partition function zeros to assess HP protein foldability is novel.

## Key findings

- Significant crossovers in thermal transitions indicate slow folding behavior.
- Absence of crossovers characterizes good protein folders.
- Kinetic Monte Carlo simulations validate the foldability criterion.

## Abstract

The heat capacity decomposition method, a well-established analytical approach in polymer thermodynamics for elucidating thermal transitions in homogeneous polymers, is extended here to heterogeneous systems. We demonstrate that the decomposition of heat capacity based on partition function zeros allows the identification of transition-like crossovers originating from compact low-energy states, thereby enabling the evaluation of the foldability of HP sequences. The occurrence of significant crossovers between the collapse and folding transitions indicates slow folding behavior, whereas their absence characterizes good folders. This criterion is further validated through kinetic Monte Carlo simulations of two representative sequences.