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Protein Dynamism and Evolvability

The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures. We consider an alternative, “avant-garde view” in which proteins are conformationally dynamic and exhibit functional promiscuity. We surmise that these properties are the foundation stones of protein evolvability; they facilitate the divergence of new functions within existing folds and the evolution of entirely new folds. Packing modes of proteins also affect their evolvability, and poorly packed, disordered, and conformationally diverse proteins may exhibit high evolvability. This dynamic view of protein structure, function, and evolvability is extrapolated to describe hypothetical scenarios for the evolution of the early proteins and future research directions in the area of protein dynamism and evolution.

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Classifications


Resource Type: Journal article/Issue, Diagram, Review
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Professional (degree program), Continuing education

Author and Copyright


Authors and Editors: Nobuhiko Tokuriki of Department of Biological Chemistry, Weizmann Institute of Science, Dan S. Tawfik of Weizmann Institute of Science
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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American Association for the Advancement of Science


     
   

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