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Lipid Binding by Disordered Proteins

External protocol Created on 30 Apr 2014

Authors

Yolanda Perez, Mariano Maffei, Irene Amata, Miguel Arbesú & Miquel Pons

Summary

Intrinsically disordered proteins (IDPs) play important roles in a multitude of biological process, especially in the regulation of signal transduction pathways. Many IDPs are implicated in several diseases such as cancer, diabetes, neurodegenerative diseases and others. We have developed a detailed protocol for purifying the intrinsically disordered Unique domain of the human non-receptor tyrosine kinase c-Src. Moreover, here we introduce two additional techniques that have been used to assess the capability of the protein to binding lipids: a simple protein-lipid assay (Echelon Lipid StripTM) and a NMR approach where we have observed the unfolded Unique domain of c-Src in the presence of different types of bicelles.

Further details

The protocol was published on Protocol Exchange on 18 December 2013. To see the entire protocol, click on the source link.

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