Protein Geometry, Function and Mutation

TL;DR

This survey reviews mathematical approaches to protein geometry and function, highlighting a postulate that secondary structure influences mutation patterns, with implications for viral glycoproteins like SARS-CoV-2.

Contribution

It introduces a novel postulate linking protein secondary structure to mutation regulation, supported by mathematical and biological insights.

Findings

Hydrogen bonds in critical regions prevent mutations.

Regions lacking backbone hydrogen bonds are more prone to mutation.

The work connects protein structure to evolutionary mutation patterns.

Abstract

This survey for mathematicians summarizes several works by the author on protein geometry and protein function with applications to viral glycoproteins in general and the spike glycoprotein of the SARS-CoV-2 virus in particular. Background biology and biophysics are sketched. This body of work culminates in a postulate that protein secondary structure regulates mutation, with backbone hydrogen bonds materializing in critical regions to avoid mutation, and disappearing from other regions to enable it.