| Range |
20 - 65 %
|
| Organism |
Budding yeast Saccharomyces cerevisiae |
| Reference |
Drummond DA, Bloom JD, Adami C, Wilke CO, Arnold FH. Why highly expressed proteins evolve slowly. Proc Natl Acad Sci U S A. 2005 Oct 4 102(40):14338-43. DOI: 10.1073/pnas.0504070102 p.14342 right column bottom paragraphPubMed ID16176987
|
| Primary Source |
[37] Bloom JD et al., Thermodynamic prediction of protein neutrality. Proc Natl Acad Sci U S A. 2005 Jan 18 102(3):606-11. DOI: 10.1073/pnas.0406744102 [45] Guo HH, Choe J, Loeb LA. Protein tolerance to random amino acid change. Proc Natl Acad Sci U S A. 2004 Jun 22 101(25):9205-10. DOI: 10.1073/pnas.0403255101PubMed ID15644440, 15197260
|
| Comments |
P.14342 right column bottom paragraph: "How large are the costs underlying translational robustness? [Investigators] can make a crude general estimate. As mentioned above, ≈19% of average-length yeast proteins will contain a missense error at typical ribosomal error rates. For diverse proteins, 20-65% of amino acid substitutions lead to inactivation (primary sources), generally due to misfolding (primary source 37). Consequently, 4-12% of a typical protein species would be expected to misfold because of missense errors." |
| Entered by |
Uri M |
| ID |
113375 |