Membrane proteins—together with lipids—make up biological membranes that are essential for life. In order to understand the role of membrane proteins in assisting membranes to carry out many different functions, it is of great importance to understand the structure of those proteins.
Membrane protein is generally soluble only in the presence of micelles, with varying amounts of lipids bound to the hydrophobic domain; thus, it is very difficult to characterize the oligomerization state of the membrane protein in a lipid-containing solvent. In this application note we demonstrate the use of multi-angle light scattering (MALS) detection in combination with UV absorption and differential refractive index (dRI) detection to determine the molar masses (MW) of both the core protein and the entire protein-lipid complex.
