Chapter title |
Analysis of Protein–Lipid Interactions Using Purified C2 Domains
|
---|---|
Chapter number | 14 |
Book title |
Plant Signal Transduction
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3115-6_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3114-9, 978-1-4939-3115-6
|
Authors |
Jessica Pérez-Sancho, Arnaldo L. Schapire, Miguel A. Botella, Abel Rosado |
Abstract |
C2 domains (C2s) are regulatory protein modules identified in eukaryotic proteins targeted to cell membranes. C2s were initially characterized as independently folded Ca(2+)-dependent phospholipids binding domains; however, later studies have shown that C2s have evolutionarily diverged into Ca(2+)-dependent and Ca(2+)-independent forms. These forms interact and regulate their affinity to diverse lipid species using different binding mechanisms. In this protocol we describe a biochemical approach to produce, purify, and solubilize functional C2 domains bound to GST for the identification of their putative Ca(2+)-dependent and Ca(2+)-independent lipid-binding partners. |
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Demographic breakdown
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Professor | 1 | 8% |
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