A Designed Phenylalanyl-tRNA Synthetase Variant Allows Efficient in Vivo Incorporation of Aryl Ketone Functionality into Proteins
Author:
Affiliation:
1. Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, Division of Biology, Biochemistry Option, California Institute of Technology, Pasadena, California 91125
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja0177096
Reference21 articles.
1. Unnatural amino acids as probes of protein structure and function
2. Towards New Protein Engineering: In Vivo Building and Folding of Protein Shuttles for Drug Delivery and Targeting by the Selective Pressure Incorporation (SPI) Method
3. Development of Strategies for the Site-Specific In Vivo Incorporation of Photoreactive Amino Acids: p-Azidophenylalanine, p-Acetylphenylalanine and Benzofuranylalanine
4. Fluorinated Coiled-Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability
5. Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids
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