scholarly journals Correction to Efficient Site-Specific Prokaryotic and Eukaryotic Incorporation of Halotyrosine Amino Acids into Proteins

2020 ◽  
Author(s):  
Hyo Sang Jang ◽  
Xiaodong Gu ◽  
Richard B. Cooley ◽  
Joseph J. Porter ◽  
Rachel L. Henson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Site Specific

scholarly journals Biosynthetic production of 13C-labeled amino acids with site-specific enrichment.

1982 ◽  
Vol 257 (3) ◽  
pp. 1224-1230
Author(s):  
D.M. LeMaster ◽  
J.E. Cronan
Keyword(s):  
Amino Acids ◽  
Site Specific

scholarly journals Identification of the target amino acids in the site-specific inactivation of triose phosphate isomerase by ferrate anion.

1983 ◽  
Vol 258 (21) ◽  
pp. 13148-13154 ◽  
Author(s):  
J Steczko ◽  
M Hermodson ◽  
B Axelrod ◽  
E Dziembor-Kentzer
Keyword(s):  
Amino Acids ◽  
Triose Phosphate Isomerase ◽  
Site Specific ◽  
Triose Phosphate

ChemInform Abstract: Synthesis and Site-Specific Incorporation of Red-Shifted Azobenzene Amino Acids into Proteins.

ChemInform ◽  
2016 ◽  
Vol 47 (19) ◽  
Author(s):  
Alford A. John ◽  
Carlo P. Ramil ◽  
Yulin Tian ◽  
Gang Cheng ◽  
Qing Lin
Keyword(s):  
Amino Acids ◽  
Site Specific

Site-specific mutagenesis with unnatural amino acids

1989 ◽  
Vol 14 (10) ◽  
pp. 400-403 ◽  
Author(s):  
Spencer J. Anthony-Cahill ◽  
Michael C. Griffith ◽  
Christopher J. Noren ◽  
Daniel J. Suich ◽  
Peter G. Schultz
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Site Specific

Stereoselective and Site-Specific Allylic Alkylation of Amino Acids and Small Peptides via a Pd/Cu Dual Catalysis

2017 ◽  
Vol 139 (29) ◽  
pp. 9819-9822 ◽  
Author(s):  
Xiaohong Huo ◽  
Rui He ◽  
Jingke Fu ◽  
Jiacheng Zhang ◽  
Guoqiang Yang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Allylic Alkylation ◽  
Small Peptides ◽  
Site Specific ◽  
Dual Catalysis

Engineering an acetyllysine reader with photocrosslinking amino acid for interactome profiling

2021 ◽  
Author(s):  
Babu Sudhamalla ◽  
Anirban Roy ◽  
Soumen Barman ◽  
Jyotirmayee Padhan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Interactions ◽  
Unnatural Amino Acids ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Powerful Approach

The site-specific installation of light-activable crosslinker unnatural amino acids offers a powerful approach to trap transient protein-protein interactions both in vitro and in vivo. Herein, we engineer a bromodomain to...

scholarly journals Site-Specific Incorporation of Unnatural Amino Acids into Escherichia coli Recombinant Protein: Methodology Development and Recent Achievement

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 255 ◽  
Author(s):  
Sviatlana Smolskaya ◽  
Yaroslav Andreev
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Nonsense Suppression ◽  
Expression Vectors ◽  
Site Specific ◽  
Suppressor Trna ◽  
E Coli ◽  
Orthogonal Pair

More than two decades ago a general method to genetically encode noncanonical or unnatural amino acids (NAAs) with diverse physical, chemical, or biological properties in bacteria, yeast, animals and mammalian cells was developed. More than 200 NAAs have been incorporated into recombinant proteins by means of non-endogenous aminoacyl-tRNA synthetase (aa-RS)/tRNA pair, an orthogonal pair, that directs site-specific incorporation of NAA encoded by a unique codon. The most established method to genetically encode NAAs in Escherichia coli is based on the usage of the desired mutant of Methanocaldococcus janaschii tyrosyl-tRNA synthetase (MjTyrRS) and cognate suppressor tRNA. The amber codon, the least-used stop codon in E. coli, assigns NAA. Until very recently the genetic code expansion technology suffered from a low yield of targeted proteins due to both incompatibilities of orthogonal pair with host cell translational machinery and the competition of suppressor tRNA with release factor (RF) for binding to nonsense codons. Here we describe the latest progress made to enhance nonsense suppression in E. coli with the emphasis on the improved expression vectors encoding for an orthogonal aa-RA/tRNA pair, enhancement of aa-RS and suppressor tRNA efficiency, the evolution of orthogonal EF-Tu and attempts to reduce the effect of RF1.

scholarly journals Decoupling Protein Production from Cell Growth Enhances the Site-Specific Incorporation of Noncanonical Amino Acids in E. coli

2020 ◽  
Vol 9 (11) ◽  
pp. 3052-3066
Author(s):  
Meritxell Galindo Casas ◽  
Patrick Stargardt ◽  
Juergen Mairhofer ◽  
Birgit Wiltschi
Keyword(s):  
Amino Acids ◽  
Cell Growth ◽  
Protein Production ◽  
Noncanonical Amino Acids ◽  
Site Specific ◽  
E Coli
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