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Why Ubiquitin Has Not Evolved

Corning Inc., Division Science &Technology, Corning, New York, NY 14831, USA
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2017, 18(9), 1995;
Received: 27 July 2017 / Revised: 28 August 2017 / Accepted: 5 September 2017 / Published: 16 September 2017
(This article belongs to the Special Issue Ubiquitin System)
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, 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
Keywords: intracellular protein degradation; deubiquitinating enzymes; self-organization; allostery; network kinetics intracellular protein degradation; deubiquitinating enzymes; self-organization; allostery; network kinetics
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MDPI and ACS Style

Allan, D.C.; Phillips, J.C. Why Ubiquitin Has Not Evolved. Int. J. Mol. Sci. 2017, 18, 1995.

AMA Style

Allan DC, Phillips JC. Why Ubiquitin Has Not Evolved. International Journal of Molecular Sciences. 2017; 18(9):1995.

Chicago/Turabian Style

Allan, Douglas C., and James C. Phillips 2017. "Why Ubiquitin Has Not Evolved" International Journal of Molecular Sciences 18, no. 9: 1995.

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