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Dynamic New World: Refining Our View of Protein Structure, Function and Evolution
Proteomes 2014, 2(2), 154-168; doi:10.3390/proteomes2020154

Origination of the Protein Fold Repertoire from Oily Pluripotent Peptides

Molecular Foundry, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720,USA
Received: 17 December 2013 / Revised: 27 February 2014 / Accepted: 20 March 2014 / Published: 25 March 2014
(This article belongs to the Special Issue Feature Paper 2013)
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While the repertoire of protein folds that exists today underlies most of life’s capabilities, our mechanistic picture of protein fold origination is incomplete. This paper discusses a hypothetical mechanism for the emergence of the protein fold repertoire from highly dynamic and collapsed peptides, exemplified by peptides with high oil content or hydrophobicity. These peptides are called pluripotent to emphasize their capacity to evolve into numerous folds transiently available to them. As evidence, the paper will discuss previous simulation work on the superior fold evolvability of oily peptides, trace (“fossil”) evidence within proteomes seen today, and a general relationship between protein dynamism and evolvability. Aside from implications on the origination of protein folds, the hypothesis implies that the vanishing utility of a random peptide in protein origination may be relatively exaggerated, as some random peptides with a certain composition (e.g., oily) may fare better than others. In later sections, the hypothesis is discussed in the context of existing discussions regarding the spontaneous origination of biomolecules.
Keywords: pluripotent hypothesis; protein fold invention; oily peptides; origins of life pluripotent hypothesis; protein fold invention; oily peptides; origins of life
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Mannige, R.V. Origination of the Protein Fold Repertoire from Oily Pluripotent Peptides. Proteomes 2014, 2, 154-168.

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