Molecular Evolution Directs Protein Translation Using Unnatural Amino Acids

Vanessa E. Cox1, Eric A. Gaucher2

1 School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, 2 School of Biology, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta
Publication Name:  Current Protocols in Chemical Biology
Unit Number:   
DOI:  10.1002/9780470559277.ch150115
Online Posting Date:  December, 2015
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Unnatural amino acids have in recent years established their importance in a wide range of fields, from pharmaceuticals to polymer science. Unnatural amino acids can increase the number of chemical groups within proteins and thus expand or enhance biological function. Our ability to utilize these important building blocks, however, has been limited by the inherent difficulty in incorporating these molecules into proteins. To address this challenge, researchers have examined how the canonical twenty amino acids are incorporated, regulated, and modified in nature. This review focuses on achievements and techniques used to engineer the ribosomal protein‚Äźtranslation machinery, including the introduction of orthogonal translation components, how directed evolution enhances the incorporation of unnatural amino acids, and the potential utility of ancient biomolecules for this process. ¬© 2015 by John Wiley & Sons, Inc.

Keywords: unnatural amino acid; directed evolution; protein translation; ancestral proteins; protein engineering

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Table of Contents

  • Introduction
  • Translation of Unnatural Amino Acids
  • Orthogonal Translation Components
  • Directed Evolution
  • Higher‐Order Directed Evolution
  • Conclusion
  • Literature Cited
  • Figures
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Literature Cited

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