Protein folding as a jamming transition

TL;DR

This paper introduces a geometric all-atom model for protein folding that explains core packing and reveals a jamming transition driven by hydrophobic interactions, accurately reproducing native protein structures.

Contribution

It presents a novel geometric model that captures the universal core packing fraction and the jamming transition in protein folding.

Findings

Identifies a universal core packing fraction of 0.55 in proteins.

Shows a jamming transition occurs with increased hydrophobic interactions.

Recapitulates native-like structures from partially unfolded states.

Abstract

Proteins fold to a specific functional conformation with a densely packed hydrophobic core that controls their stability. We develop a geometric, yet all-atom model for proteins that explains the universal core packing fraction of $\phi_c=0.55$ found in experimental measurements. We show that as the hydrophobic interactions increase relative to the temperature, a novel jamming transition occurs when the core packing fraction exceeds $\phi_c$. The model also recapitulates the global structure of proteins since it can accurately refold to native-like structures from partially unfolded states.