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Method Article
Expressed Protein Ligation using subtiligase
Philip Cole
Department of Pharmacology and Molecular and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD, USA
Corresponding Author
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Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-Cys containing peptides but the requirement of a Cys residue at the ligation junction can limit its use. Here we present a method that employs subtiligase to efficiently ligate Cys-free peptides to protein thioesters.
Keywords
Semisynthesis, Expressed Protein Ligation, EPL, Protein thioester
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Biochemistry
Associated Publications
Enzyme-catalyzed expressed protein ligation
by Samuel H Henager, Nam Chu, Zan Chen, +5
Nature Methods (19 October, 2016)
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This is a preprint. It has not completed peer review.
Method Article
Expressed Protein Ligation using subtiligase
Philip Cole
Department of Pharmacology and Molecular and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD, USA
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
History
CURRENT STATUS: Posted
Version 1
Posted 19 Oct, 2016
No community comments so far
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
Subject Areas
Biochemistry
License:
This work is licensed under a CC BY-NC 3.0 License. Read Full License
Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-Cys containing peptides but the requirement of a Cys residue at the ligation junction can limit its use. Here we present a method that employs subtiligase to efficiently ligate Cys-free peptides to protein thioesters.
Figure 1
Figure 2
Associated Publications
Enzyme-catalyzed expressed protein ligation
by Samuel H Henager, Nam Chu, Zan Chen, +5
Nature Methods (19 October, 2016)