Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5102379 | Physica A: Statistical Mechanics and its Applications | 2018 | 5 Pages |
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 correlated long-range 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.
Related Topics
Physical Sciences and Engineering
Mathematics
Mathematical Physics
Authors
Douglas C. Allan, J.C. Phillips,