Why Ubiquitin Has Not Evolved
AbstractUbiquitin, 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, indicating that ubiquitin is perfect. Key features of its functionality are identified here using critical point thermodynamic scaling theory. These include synchronized pivots and hinges, a stabilizing central pivot, and Fano interference between first- and second-order elements of correlated long-range (allosteric) globular surface shape transitions. Comparison with its closest relative, 76 amino acid Nedd8, shows that the latter lacks all these features. A cracked elastic network model is proposed for the common target shared by many diseased proteins. View Full-Text
Share & Cite This Article
Allan, D.C.; Phillips, J.C. Why Ubiquitin Has Not Evolved. Int. J. Mol. Sci. 2017, 18, 1995.
Allan DC, Phillips JC. Why Ubiquitin Has Not Evolved. International Journal of Molecular Sciences. 2017; 18(9):1995.Chicago/Turabian Style
Allan, Douglas C.; Phillips, James C. 2017. "Why Ubiquitin Has Not Evolved." Int. J. Mol. Sci. 18, no. 9: 1995.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.