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Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins

[Image: see text] Here, we report the site-specific incorporation of a thioester containing noncanonical amino acid (ncAA) into recombinantly expressed proteins. Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an...

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Autores principales: Xuan, Weimin, Collins, Daniel, Koh, Minseob, Shao, Sida, Yao, Anzhi, Xiao, Han, Garner, Philip, Schultz, Peter G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5856652/
https://www.ncbi.nlm.nih.gov/pubmed/29360343
http://dx.doi.org/10.1021/acschembio.7b00998
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author Xuan, Weimin
Collins, Daniel
Koh, Minseob
Shao, Sida
Yao, Anzhi
Xiao, Han
Garner, Philip
Schultz, Peter G.
author_facet Xuan, Weimin
Collins, Daniel
Koh, Minseob
Shao, Sida
Yao, Anzhi
Xiao, Han
Garner, Philip
Schultz, Peter G.
author_sort Xuan, Weimin
collection PubMed
description [Image: see text] Here, we report the site-specific incorporation of a thioester containing noncanonical amino acid (ncAA) into recombinantly expressed proteins. Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair. To demonstrate the utility of ThioD, we used native chemical ligation to label green fluorescent protein with a fluorophore in good yield.
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spelling pubmed-58566522018-03-16 Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins Xuan, Weimin Collins, Daniel Koh, Minseob Shao, Sida Yao, Anzhi Xiao, Han Garner, Philip Schultz, Peter G. ACS Chem Biol [Image: see text] Here, we report the site-specific incorporation of a thioester containing noncanonical amino acid (ncAA) into recombinantly expressed proteins. Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair. To demonstrate the utility of ThioD, we used native chemical ligation to label green fluorescent protein with a fluorophore in good yield. American Chemical Society 2018-01-23 2018-03-16 /pmc/articles/PMC5856652/ /pubmed/29360343 http://dx.doi.org/10.1021/acschembio.7b00998 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Xuan, Weimin
Collins, Daniel
Koh, Minseob
Shao, Sida
Yao, Anzhi
Xiao, Han
Garner, Philip
Schultz, Peter G.
Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title_full Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title_fullStr Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title_full_unstemmed Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title_short Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins
title_sort site-specific incorporation of a thioester containing amino acid into proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5856652/
https://www.ncbi.nlm.nih.gov/pubmed/29360343
http://dx.doi.org/10.1021/acschembio.7b00998
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