| Chapter title |
Analysis of Protein Tyrosine Kinase Specificity Using Positional Scanning Peptide Microarrays.
|
|---|---|
| Chapter number | 3 |
| Book title |
Peptide Microarrays
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-3037-1_3 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-3036-4, 978-1-4939-3037-1
|
| Authors |
Yang Deng, Benjamin E. Turk |
| Editors |
Marina Cretich, Marcella Chiari |
| Abstract |
Protein tyrosine kinases phosphorylate their substrates within the context of specific consensus sequences surrounding the site of modification. We describe a peptide microarray approach to rapidly determine tyrosine kinase phosphorylation site motifs. This method uses a peptide library that systematically substitutes each of the amino acid residues at multiple positions surrounding a central tyrosine residue. Peptide substrates are synthesized as biotin conjugates for immobilization on avidin-coated slides. Following incubation of the slide with protein kinase and radiolabeled ATP, the relative extent of phosphorylation of each of the peptides is quantified by phosphor imaging. This method allows small quantities of kinase to be analyzed rapidly in parallel, facilitating analysis of large numbers of kinases. |
Mendeley readers
Geographical breakdown
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|---|---|---|
| Unknown | 5 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
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| Researcher | 1 | 20% |
| Other | 1 | 20% |
| Unknown | 2 | 40% |
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|---|---|---|
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| Unknown | 3 | 60% |