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Int. J. Mol. Sci. 2017, 18(9), 1995; doi:10.3390/ijms18091995

Why Ubiquitin Has Not Evolved

1
Corning Inc., Division Science &Technology, Corning, New York, NY 14831, USA
2
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA
*
Author to whom correspondence should be addressed.
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)
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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, 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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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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

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