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A general method for site-specific incorporation of unnatural amino acids into proteins

Academic Article
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Overview

authors

  • Noren, C. J.
  • Anthony-Cahill, S. J.
  • Griffith, M. C.
  • Schultz, Peter

publication date

  • April 1989

journal

  • Science  Journal

abstract

  • A new method has been developed that makes it possible to site-specifically incorporate unnatural amino acids into proteins. Synthetic amino acids were incorporated into the enzyme beta-lactamase by the use of a chemically acylated suppressor transfer RNA that inserted the amino acid in response to a stop codon substituted for the codon encoding residue of interest. Peptide mapping localized the inserted amino acid to a single peptide, and enough enzyme could be generated for purification to homogeneity. The catalytic properties of several mutants at the conserved Phe66 were characterized. The ability to selectively replace amino acids in a protein with a wide variety of structural and electronic variants should provide a more detailed understanding of protein structure and function.

subject areas

  • Amino Acids
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli
  • Mutation
  • Protein Biosynthesis
  • Proteins
  • RNA, Transfer
  • beta-Lactamases
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2649980

PubMed ID

  • 2649980
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Additional Document Info

start page

  • 182

end page

  • 188

volume

  • 244

issue

  • 4901

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