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Protein Synthesis pp 325–354Cite as

Protein Engineering with Nonstandard Amino Acids

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 77))

Abstract

Site-directed mutagenesis has become an extremely powerful tool for the study of protein folding, protein-protein interactions, enzymatic catalysis, and other structure-function issues. Whereas this technique has had a major impact, it nonetheless has been limited to the 20 “proteinogenic” (standard) amino acids normally incorporated during ribosomal biosynthesis. This limitation has precluded the ability to site-specifically incorporate other amino acids that have been specifically designed to probe structure, function, or activity in novel ways. The ability to modify a protein by site-specifically introducing such non-standard amino acids with novel functionality would thus be useful in many investigations, but in addition, the ability to introduce nonstandard amino acids with more conservative modifications than are allowed by traditional site-directed mutagenesis (i.e., substitution of a single atom within an amino acid side chain) also could be quite useful.

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of California, Irvine, CA

    Lance E. Steward & A. Richard Chamberlin

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  1. Lance E. Steward
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  2. A. Richard Chamberlin
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Editors and Affiliations

  1. Blond McIndoe Center, Queen Victoria Hospital, Sussex, England

    Robin Martin

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© 1998 Humana Press Inc.

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Steward, L.E., Chamberlin, A.R. (1998). Protein Engineering with Nonstandard Amino Acids. In: Martin, R. (eds) Protein Synthesis. Methods in Molecular Biology, vol 77. Springer, Totowa, NJ. https://doi.org/10.1385/0-89603-397-X:325

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  • DOI: https://doi.org/10.1385/0-89603-397-X:325

  • Publisher Name: Springer, Totowa, NJ

  • Print ISBN: 978-0-89603-397-9

  • Online ISBN: 978-1-59259-563-1

  • eBook Packages: Springer Protocols

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