Characterization of Protein Oligomers by Multi‐Angle Light Scattering

Abstract

Numerous methods for characterizing oligomerization of proteins exist, with each of them having its advantages and limitation. Here, we focus on multi‐angle light scattering (MALS), which is one of the most efficient methods for studying the oligomerization of soluble proteins in their native form in solution. MALS can provide many important parameters such as the exact molar mass and size of the protein of interest, its hydrodynamic radius, and additional structural information. Studying protein oligomerization using Light scattering (LS) methods is combined in many cases with chromatographic methods, resulting in accurate characterization of this dynamic process with minimal measurement‐related interferences. Here, we describe several light scattering‐based techniques combined with several separation methods, focusing on the more common method of size exclusion chromatography – multi‐angle light scattering (SEC‐MALS) and two additional and in some cases complementary methods, ion exchange chromatography and flow field fractionation combined with MALS.