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
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
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.