A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.

ABSTRACT: The halophile environment has a number of compelling aspects with regard to the origin of structured polypeptides (i.e., proteogenesis) and, instead of a curious niche that living systems adapted into, the halophile environment is emerging as a candidate "cradle" for proteogenesis. In this viewpoint, a subsequent halophile-to-mesophile transition was a key step in early evolution. Several lines of evidence indicate that aromatic amino acids were a late addition to the codon table and not part of the original "prebiotic" set comprising the earliest polypeptides. We test the hypothesis that the availability of aromatic amino acids could facilitate a halophile-to-mesophile transition by hydrophobic core-packing enhancement. The effects of aromatic amino acid substitutions were evaluated in th

SUBMITTER: Longo LM 

PROVIDER: S-EPMC4282409 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature