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Proteomes 2014, 2(1), 128-153; doi:10.3390/proteomes2010128

Dynamic New World: Refining Our View of Protein Structure, Function and Evolution

Molecular Foundry, Lawrence Berkeley National Laboratory, 1 Cyclotron Road,Berkeley, CA 94720, USA
Received: 17 December 2013 / Revised: 12 February 2014 / Accepted: 20 February 2014 / Published: 7 March 2014
(This article belongs to the Special Issue Feature Paper 2013)
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Proteins are crucial to the functioning of all lifeforms. Traditional understanding posits that a single protein occupies a single structure (“fold”), which performs a single function. This view is radically challenged with the recognition that high structural dynamism—the capacity to be extra “floppy”—is more prevalent in functional proteins than previously assumed. As reviewed here, this dynamic take on proteins affects our understanding of protein “structure”, function, and evolution, and even gives us a glimpse into protein origination. Specifically, this review will discuss historical developments concerning protein structure, and important new relationships between dynamism and aspects of protein sequence, structure, binding modes, binding promiscuity, evolvability, and origination. Along the way, suggestions will be provided for how key parts of textbook definitions—that so far have excluded membership to intrinsically disordered proteins (IDPs)—could be modified to accommodate our more dynamic understanding of proteins. View Full-Text
Keywords: protein dynamism; intrinsically disordered; structure; function; promiscuity; evolution protein dynamism; intrinsically disordered; structure; function; promiscuity; evolution

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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Mannige, R.V. Dynamic New World: Refining Our View of Protein Structure, Function and Evolution. Proteomes 2014, 2, 128-153.

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