Lipid Binding by Disordered Proteins

Abstract

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 Strip TM) and a NMR approach where we have observed the unfolded Unique domain of c-Src in the presence of different types of bicelles.