Configuration Interaction of Hydropathic Waves Enables Ubiquitin Functionality

TL;DR

This paper introduces a novel thermodynamic and elastic network model to understand ubiquitin's functionality, highlighting unique wave interactions that distinguish it from related proteins and potentially target diseased proteins.

Contribution

It presents a new critical point thermodynamic scaling theory and cracked elastic network model to explain ubiquitin's functional mechanisms and differences from Nedd8.

Findings

Identification of Fano interference in ubiquitin

Distinct features compared to Nedd8

Proposal of a cracked elastic network model

Abstract

Ubiquitin, discovered less than 50 years ago, tags thousands of diseased proteins for destruction. It is small (only 76 amino acids), and is found unchanged in mammals, birds, fish and even worms. Key features of its functionality are identified here using critical point thermodynamic scaling theory. These include Fano interference between first- and second-order elements of globular surface shape transitions. Comparison with its closest relative, 76 amino acid Nedd8, shows that the latter lacks these features. A cracked elastic network model is proposed for the common target shared by many diseased proteins.