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Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.

Title: Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
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Name(s): Longo, Liam M, author
Lee, Jihun, author
Blaber, Michael, author
Type of Resource: text
Genre: journal article
text
Date Issued: 2013-02-05
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 "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.
Identifier: FSU_pmch_23341608 (IID), 10.1073/pnas.1219530110 (DOI), PMC3568330 (PMCID), 23341608 (RID), 23341608 (EID), 1219530110 (PII)
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3568330.
Subject(s): Amino Acids/chemistry
Biophysical Phenomena
Calorimetry, Differential Scanning
Crystallography, X-Ray
Evolution, Molecular
Models, Molecular
Mutagenesis
Origin of Life
Protein Folding
Protein Stability
Proteins/chemistry
Proteins/genetics
Static Electricity
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_pmch_23341608
Owner Institution: FSU
Is Part Of: Proceedings of the National Academy of Sciences of the United States of America.
1091-6490
Issue: iss. 6, vol. 110

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Longo, L. M., Lee, J., & Blaber, M. (2013). Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein. Proceedings Of The National Academy Of Sciences Of The United States Of America. Retrieved from http://purl.flvc.org/fsu/fd/FSU_pmch_23341608