A Gauge Field Theory of Chirally Folded Homopolymers with Applications to Folded Proteins

TL;DR

This paper introduces a gauge field theory-based lattice model for chiral homopolymers, successfully describing folded protein properties and matching empirical data from the Protein Data Bank.

Contribution

It develops a novel gauge invariance-based model that captures the statistical and structural features of folded proteins, linking string geometry with protein folding.

Findings

Model reproduces the compactness index of proteins in the Protein Data Bank

The low temperature phase aligns with properties of real folded proteins

Results demonstrate the model's ability to match empirical protein data

Abstract

We combine the principle of gauge invariance with extrinsic string geometry to develop a lattice model that can be employed to theoretically describe properties of chiral, unbranched homopolymers. We find that in its low temperature phase the model is in the same universality class with proteins that are deposited in the Protein Data Bank, in the sense of the compactness index. We apply the model to analyze various statistical aspects of folded proteins. Curiously we find that it can produce results that are a very good good match to the data in the Protein Data Bank.