Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 10 April 2009:
Vol. 324. no. 5924, pp. 203 - 207
DOI: 10.1126/science.1169375

Review

Protein Dynamism and Evolvability

Nobuhiko Tokuriki and Dan S. Tawfik*

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.

Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

* To whom correspondence should be addressed. E-mail: tawfik{at}weizmann.ac.il

Read the Full Text



THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Predicting Virus Evolution: The Relationship between Genetic Robustness and Evolvability of Thermotolerance.
C.B. Ogbunugafor, R.C. Mcbride, and P.E. Turner (2009)
Cold Spring Harb Symp Quant Biol
   Abstract »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)