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Simplified Protein Design Biased for Pre-Biotic Amino Acids Yields a Foldable, Halophilic Protein

Title: Simplified Protein Design Biased for Pre-Biotic Amino Acids Yields a Foldable, Halophilic Protein.
Name(s): Longo, Liam, author
Lee, Jihun, author
Blaber, Michael, author
Type of Resource: text
Genre: text
Date Issued: 2012-12-19
Physical Form: computer
Physical Form: online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 “pre-biotic” -amino acids. Prior to the emergence of biosynthetic pathways this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this pre-biotic set is whether it defines a “foldable set”? - that is, does it contain sufficient chemical information to permit cooperatively-folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions two “primitive” versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of pre-biotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the pre-biotic amino acids do comprise a foldable set within the halophile environment.
Identifier: FSU_libsubv1_scholarship_submission_1456500856 (IID), 10.1073/pnas.1219530110 (DOI)
Keywords: Primordial, Primitive, Protein simplification, β-trefoil, Proteogenesis, Abiogenesis
Persistent Link to This Record:
Owner Institution: FSU
Is Part Of: Proceedings of the National Academy of Sciences USA.
Issue: iss. no. 6, vol. 110