Summary
Proteins with higher thermostability are more capable of laboratory evolution new functions; e.g., they are more evolvable (1). This was determined using cytochrome P450, where stabilizing mutations acted as a buffer against destabilizing mutations.
Details
Additionally, (2) found that evolving YFP to GFP had greater overall success and greater fitness if starting from YFP that was under greater selective pressure in prior rounds:
populations under strong selection for the ancestral yellow fluorescent phenotype during phase I subsequently evolved the new green fluorescent phenotype most rapidly during phase II. Compared to populations under weak or no selection, they reached higher green fluorescence during each generation of phase II and evolved a green emission peak more rapidly
See also
- Ancestrally reconstructed sequences are more thermostable than extant sequences
- Ancestral sequence reconstruction
- The majority of missense mutations are destabilizing