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Multiple‐Site Labeling of Proteins with Unnatural Amino Acids
Author(s) -
Loscha Karin V.,
Herlt Anthony J.,
Qi Ruhu,
Huber Thomas,
Ozawa Kiyoshi,
Otting Gottfried
Publication year - 2012
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.201108275
Subject(s) - amino acid , phenylalanine , transfer rna , chemistry , protein biosynthesis , nuclear magnetic resonance spectroscopy , biochemistry , stereochemistry , aminoacyl trna synthetase , cell free protein synthesis , rna , gene
A cell‐free protein synthesis system from which the release factor RF1 has been selectively removed enables the facile incorporation of unnatural amino acids into proteins at difficult and multiple sites by optimized use of orthogonal tRNA/aminoacyl‐tRNA synthetase systems. 19 F NMR spectroscopy of a protein labeled combinatorially with trifluoromethyl phenylalanine (red in picture) at multiple sites establishes resonance assignments with a minimal number of samples.