| Range |
~1.3 (~5.5 kJ/mol) kcal/mol
|
| Organism |
Generic |
| Reference |
Tokuriki N, Stricher F, Serrano L, Tawfik DS. How protein stability and new functions trade off. PLoS Comput Biol. 2008 Feb 29 4(2):e1000002. doi: 10.1371/journal.pcbi.1000002. p.1 abstractPubMed ID18463696
|
| Method |
"[Researchers] performed a comprehensive analysis of
the type, location, and stability effects of mutations that
have conferred new enzymatic functions in laboratory
evolution experiments." |
| Comments |
"[Researchers] found that mutations that modulate enzymatic functions are mostly destabilizing (average ??G = +0.9 kcal/mol), and are almost as destabilizing as the "average" mutation in these enzymes (+1.3 kcal/mol)." |
| Entered by |
Uri M |
| ID |
109549 |