Document Detail


Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
MedLine Citation:
PMID:  23341608     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 "prebiotic" α-amino acids. Before 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 prebiotic 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 prebiotic 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 prebiotic amino acids do comprise a foldable set within the halophile environment.
Authors:
Liam M Longo; Jihun Lee; Michael Blaber
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-01-22
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  110     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-06     Completed Date:  2013-04-09     Revised Date:  2013-08-09    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2135-9     Citation Subset:  IM    
Affiliation:
Department of Biomedical Sciences, Florida State University, Tallahassee, FL 32306-4300, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/3Q7W;  3Q7X;  4D8H
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / chemistry*
Biogenesis
Biophysical Phenomena
Calorimetry, Differential Scanning
Crystallography, X-Ray
Evolution, Molecular*
Models, Molecular
Mutagenesis
Protein Folding
Protein Stability
Proteins / chemistry*,  genetics
Static Electricity
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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