Configuration Interaction of Hydropathic Waves Enables Ubiquitin Functionality

2016/11/11 by Douglas C. Allan, Allan, Douglas C., J. C. Phillips +1
Biochemistry, Genetics and Molecular Biology · #FOS: Biological sciences #Hemoglobin structure and function #Microtubule and mitosis dynamics #Other Quantitative Biology (q-bio.OT) #Protein Structure and Dynamics #q-bio.OT

paper · pdf · doi:10.48550/arxiv.1611.03818

11pages, 4 figures

arxiv created 2016/11/11 · openalex publication_date 2016/11/11 · arxiv updated 2016/11/14 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28

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.

Citations

• A simple method for displaying the hydropathic character of a protein
• The Ubiquitin Code
• Effects of Configuration Interaction on Intensities and Phase Shifts

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• Self-Organized Criticality in Proteins: Hydropathic Roughening Profiles of G-Protein Coupled Receptors
• Hydroanalysis of Animal Lysozymes c and Human Defensins a
• An edge β‐strand mutation turns ubiquitin into a pore‐forming amyloid
• The Ubiquitin Script: writing protein fates in chains
• Protein Sequence, Structure, Stability and Functionality