Multimeranalízis

Multimeranalízis, often translated as multimer analysis, is a technique used in biochemistry and molecular biology to study the assembly and composition of protein complexes. It involves separating molecules based on their size and shape, specifically focusing on how individual protein subunits associate to form larger structures called multimers. These multimers can range from simple dimers (two subunits) to more complex oligomers.

The primary goal of multimer analysis is to determine if a protein exists as a monomer, dimer, or a higher-order multimer, and to identify the specific subunits involved in these complexes. This information is crucial for understanding protein function, as many biological processes rely on the cooperative action of proteins within a multimeric assembly. For example, enzyme activity, signal transduction, and structural integrity often depend on the formation of specific protein complexes.

Various experimental methods can be employed for multimer analysis. Size exclusion chromatography (SEC) separates molecules based on their hydrodynamic radius, allowing larger multimeric forms to elute earlier than monomers. Dynamic light scattering (DLS) measures the size of particles in solution by analyzing the fluctuations in scattered light intensity, providing information about the average size and size distribution of protein assemblies. Analytical ultracentrifugation (AUC) is a more sophisticated technique that uses sedimentation to analyze the size, shape, and stoichiometry of macromolecular complexes. Native gel electrophoresis can also distinguish between monomers and multimers if their migration patterns differ on a non-denaturing gel. These methods collectively provide insights into the quaternary structure of proteins.