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PMID: 16689635 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Review

Expanding the genetic code.

Annual review of biophysics and biomolecular structure ·Vol. 35 ·2006-00-00 ·Pages 225-49

Wang L, Xie J, Schultz PG

Abstract

Recently, a general method was developed that makes it possible to genetically encode unnatural amino acids with diverse physical, chemical, or biological properties in Escherichia coli, yeast, and mammalian cells. More than 30 unnatural amino acids have been incorporated into proteins with high fidelity and efficiency by means of a unique codon and corresponding tRNA/aminoacyl-tRNA synthetase pair. These include fluorescent, glycosylated, metal-ion-binding, and redox-active amino acids, as well as amino acids with unique chemical and photochemical reactivity. This methodology provides a powerful tool both for exploring protein structure and function in vitro and in vivo and for generating proteins with new or enhanced properties.

MeSH Terms
Amino Acid Substitution Amino Acids/chemistry,genetics Animals Directed Molecular Evolution/methods Evolution, Molecular Genetic Code/genetics Humans Mutagenesis, Site-Directed/methods Mutation Protein Engineering/methods Proteins/chemistry,genetics Structure-Activity Relationship
Chemicals
Amino Acids Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wang Lei
The Jack H. Skirball Center for Chemical Biology & Proteomics, The Salk Institute for Biological Studies, La Jolla, California 92037, USA.
Xie Jianming
Schultz Peter G
Article Info
Journal
Annual review of biophysics and biomolecular structure
Abbr.
Annu Rev Biophys Biomol Struct
ISSN
1056-8700
Published
2006-00-00
Pages
225-49
Language
English
Region
United States
NLM ID
9211097
Subset
IM
Grants
NIGMS NIH HHS · GM-62159 · United States
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