Abstract
Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-terminal cysteine (N-Cys)-containing peptides, but the requirement of a Cys residue at the ligation junction can limit the utility of this method. Here we employ subtiligase variants to efficiently ligate Cys-free peptides to protein thioesters. Using this method, we have more accurately determined the effect of C-terminal phosphorylation on the tumor suppressor protein PTEN.
Original language | English (US) |
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Pages (from-to) | 925-927 |
Number of pages | 3 |
Journal | Nature Methods |
Volume | 13 |
Issue number | 11 |
DOIs | |
State | Published - Nov 1 2016 |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Cell Biology