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Curr Opin Struct Biol. 2014 Jun;26:131-8. doi: 10.1016/j.sbi.2014.06.007. Epub 2014 Jul 17.

The robustness and innovability of protein folds.

Author information

1
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
2
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: dan.tawfik@weizmann.ac.il.

Abstract

Assignment of protein folds to functions indicates that >60% of folds carry out one or two enzymatic functions, while few folds, for example, the TIM-barrel and Rossmann folds, exhibit hundreds. Are there structural features that make a fold amenable to functional innovation (innovability)? Do these features relate to robustness--the ability to readily accumulate sequence changes? We discuss several hypotheses regarding the relationship between the architecture of a protein and its evolutionary potential. We describe how, in a seemingly paradoxical manner, opposite properties, such as high stability and rigidity versus conformational plasticity and structural order versus disorder, promote robustness and/or innovability. We hypothesize that polarity--differentiation and low connectivity between a protein's scaffold and its active-site--is a key prerequisite for innovability.

PMID:
25038399
DOI:
10.1016/j.sbi.2014.06.007
[Indexed for MEDLINE]

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