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Prebiotic Protein Design supports a Halophile Origin of Foldable Proteins

Title: Prebiotic Protein Design supports a Halophile Origin of Foldable Proteins.
Name(s): Longo, Liam, author
Blaber, Michael, author
Type of Resource: text
Genre: text
Date Issued: 2014-01-06
Physical Form: computer
Physical Form: online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: In this opinion article we argue for the following: 1) 10 of the common α-amino acids were likely available in the prebiotic world, produced by a variety of abiotic chemical syntheses; 2) although a highly-restricted set, experimental and theoretical considerations indicates this prebiotic alphabet of α-amino acids contains the requisite chemical information to comprise a foldable set (i.e., foldable polypeptides are possible having a composition only of the prebiotic alphabet); 3) a comparison of the prebiotic alphabet with known proteomes predicts that polypeptides comprised of the prebiotic alphabet would have halophile properties – i.e., folding and solubility would be compatible with high salt. Recent experimental studies support this hypothesis; 4) proteogenesis (the emergence of polypeptides) – a key aspect of abiogenesis (the emergence of life from non-living molecules) – is likely to have occurred within the halophile environment.
Identifier: FSU_libsubv1_scholarship_submission_1456502085 (IID), 10.3389/fmicb.2013.00418 (DOI)
Keywords: Abiogenesis, Halophile, Protein evolution, Prebiotic, Protein folding, Protein design
Persistent Link to This Record:
Owner Institution: FSU
Is Part Of: Frontiers in Microbiology.
Issue: vol. 4