Protein design at the interface of the pre-biotic and biotic worlds

[Display omitted] ► A consensus set of 10 pre-biotic α-amino acids is identified from diverse abiotic sources. ► The properties of the pre-biotic set of amino acids suggest that it likely comprises a “foldable” set. ► Proteogenesis appears most compatible with an acidophilic/halophilic environment....

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Published in:Archives of biochemistry and biophysics Vol. 526; no. 1; pp. 16 - 21
Main Authors: Longo, Liam M., Blaber, Michael
Format: Journal Article
Language:English
Published: United States Elsevier Inc 01-10-2012
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Summary:[Display omitted] ► A consensus set of 10 pre-biotic α-amino acids is identified from diverse abiotic sources. ► The properties of the pre-biotic set of amino acids suggest that it likely comprises a “foldable” set. ► Proteogenesis appears most compatible with an acidophilic/halophilic environment. “Proteogenesis” (the origin of proteins) is a likely key event in the unsolved problem of biogenesis (the origin of life). The raw material for the very first proteins comprised the available amino acids produced and accumulated upon the early earth via abiotic chemical and physical processes. A broad consensus is emerging that this pre-biotic set likely comprised Ala, Asp, Glu, Gly, Ile, Leu, Pro, Ser, Thr, and Val. A key question in proteogenesis is whether such abiotically-produced amino acids comprise a “foldable” set. Current knowledge of protein folding identifies properties of complexity, secondary structure propensity, hydrophobic–hydrophilic patterning, core-packing potential, among others, as necessary elements of foldability. None of these requirements excludes the pre-biotic set of amino acids from being a foldable set. Moreover, nucleophile and metal ion/mineral binding capabilities also appear present in the pre-biotic set. Properties of the pre-biotic set, however, likely restrict foldability to the acidophilic/halophilic environment.
Bibliography:http://dx.doi.org/10.1016/j.abb.2012.06.009
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ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2012.06.009