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In Vivo Incorporation of Multiple Noncanonical Amino Acids into Proteins
Author(s) -
Hoesl Michael G.,
Budisa Nediljko
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201005680
Subject(s) - genetic code , recombinant dna , amino acid , computational biology , in vivo , sequence (biology) , quadruplets , coding region , amino acid residue , protein engineering , chemistry , peptide sequence , biochemistry , biology , genetics , gene , enzyme , pregnancy , gestation
Expansion of the standard genetic code enables the design of recombinant proteins with novel and unusual properties. Traditionally, such proteins have contained only a single type of noncanonical amino acid (NCAA) in their amino acid sequence. However, recently reported initial efforts demonstrate that it is possible with suppression‐based methods to translate two chemically distinct NCAAs into a single recombinant protein by combining the suppression of different termination codons and nontriplet coding units (such as quadruplets). The possibility of expanding the code with various NCAAs simultaneously further increases the toolkit for the generation of multifunctionalized proteins.