ABSTRACT
The purification of membrane proteins to near homogeneity is prerequisite to a number of analytical, spectroscopic, and structural studies. Prior to purification, the protein must be in a soluble state, that is, no longer associated with the lipid bilayer. Hence, it is necessary to disrupt the interactions between the protein and the lipid while maintaining the structural and functional integrity of the protein. This can, however, be complicated due to the requirement for particular lipid molecules for folding and due to the function of many membrane proteins.1-3 So, how do we solubilize a membrane protein while keeping all features intact? Once we have a
soluble membrane protein, how can we proceed with purification and preliminary analysis of the protein? Are there unique issues associated with the purification of membrane proteins not encountered with soluble proteins? We shall cover these and other issues in this chapter.
