The quality and ease of proteomics analysis depends on the performance of the
analytical tools used, and thus of the performances of the protein separation
tools used to deconvolute complex protein samples. Among protein samples,
membrane proteins are one of the most difficult sample classes, because of
their hydrophobicity and embedment in the lipid bilayers. This review deals
with the recent progresses and advances made in the separation of membrane
proteins by 2-DE separating only denatured proteins. Traditional 2-D methods,
i.e., methods using IEF in the first dimension are compared to methods using
only zone electrophoresis in both dimensions, i.e., electrophoresis in the
presence of cationic or anionic detergents. The overall performances and fields
of application of both types of method is critically examined, as are future
prospects for this field