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Mendeley readers
Chapter title |
Liquid Chromatography-Tandem Mass Spectrometry to Define Sortase Cleavage Products.
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Chapter number | 8 |
Book title |
Bacterial Cell Wall Homeostasis
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Published in |
Methods in molecular biology, January 2016
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DOI | 10.1007/978-1-4939-3676-2_8 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3674-8, 978-1-4939-3676-2
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Authors |
Andrew Duong, Kalinka Koteva, Danielle L. Sexton, Marie A. Elliot |
Editors |
Hee-Jeon Hong |
Abstract |
Sortase enzymes have specific endopeptidase activity, cleaving within a defined pentapeptide sequence at the C-terminal end of their protein substrates. Here, we describe how monitoring sortase cleavage activity can be achieved using peptide substrates. Peptide cleavage can be readily analyzed by liquid chromatography/tandem mass spectrometry (LC/MS/MS), which allows for the precise definition of cleavage sites. This technique could be used to analyze the peptidase activity of any enzyme, and identify sites of cleavage within any peptide. |
Mendeley readers
The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 40% |
Student > Ph. D. Student | 1 | 20% |
Professor > Associate Professor | 1 | 20% |
Other | 1 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 3 | 60% |
Agricultural and Biological Sciences | 1 | 20% |
Unknown | 1 | 20% |