Covalent bond symmetry breaking and protein secondary structure

TL;DR

This paper uncovers a universal symmetry breaking phenomenon in proteins that correlates with their secondary structures, providing new insights into protein folding and the origins of biological complexity.

Contribution

It introduces a novel symmetry breaking mechanism in proteins that links covalent bond geometry to secondary structure formation.

Findings

Symmetry breaking occurs in all biologically active proteins.

The pattern of symmetry breaking correlates with local secondary structures.

This phenomenon relates to fundamental aspects of protein folding and biological origin.

Abstract

Both symmetry and organized breaking of symmetry have a pivotal r\^ole in our understanding of structure and pattern formation in physical systems, including the origin of mass in the Universe and the chiral structure of biological macromolecules. Here we report on a new symmetry breaking phenomenon that takes place in all biologically active proteins, thus this symmetry breaking relates to the inception of life. The unbroken symmetry determines the covalent bond geometry of a sp3 hybridized carbon atom. It dictates the tetrahedral architecture of atoms around the central carbon of an amino acid. Here we show that in a biologically active protein this symmetry becomes broken. Moreover, we show that the pattern of symmetry breaking is in a direct correspondence with the local secondary structure of the folded protein.