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Stability and the Evolvability of Function in a Model Protein Jesse D. Bloom,*y
 

Summary: Stability and the Evolvability of Function in a Model Protein
Jesse D. Bloom,*y
Claus O. Wilke,y
Frances H. Arnold,z
and Christoph Adamiy§
*Department of Chemistry, y
Digital Life Laboratory; z
Division of Chemistry and Chemical Engineering;
and §
Jet Propulsion Laboratory, California Institute of Technology, Pasadena, California 91125
ABSTRACT Functional proteins must fold with some minimal stability to a structure that can perform a biochemical task. Here
we use a simple model to investigate the relationship between the stability requirement and the capacity of a protein to evolve
the function of binding to a ligand. Although our model contains no built-in tradeoff between stability and function, proteins
evolved function more efficiently when the stability requirement was relaxed. Proteins with both high stability and high function
evolved more efficiently when the stability requirement was gradually increased than when there was constant selection for high
stability. These results show that in our model, the evolution of function is enhanced by allowing proteins to explore sequences
corresponding to marginally stable structures, and that it is easier to improve stability while maintaining high function than to
improve function while maintaining high stability. Our model also demonstrates that even in the absence of a fundamental
biophysical tradeoff between stability and function, the speed with which function can evolve is limited by the stability
requirement imposed on the protein.

  

Source: Arnold, Frances H. - Division of Chemistry and Chemical Engineering, California Institute of Technology

 

Collections: Chemistry; Biology and Medicine