Characterization of a soluble library of the PAO1 membrane proteome with emphasis on c-di-GMP turnover enzymes.

Studies of protein-protein interactions in membranes are very important to fully understand the biological function of a cell. The extraction of proteins from the native membrane environment is a critical step in the preparation of membrane proteins that might affect the stability of protein complexes. In this work, we used the amphiphilic diisobutylene/maleic acid copolymer to extract the membrane proteome of the opportunistic pathogen , thereby creating a soluble membrane-protein library within a native-like lipid-bilayer environment.