Dynamic light scattering studies of protein aqueous solutions provide valuable insight regarding protein physicochemical properties such as their molecular size, the existence of different populations (oligomeric protein aggregates) in solution and their size distribution, their hydrodynamic radius and diffusion behaviour. Furthermore, the determination of the molecular weight and radius of gyration, as well as the extraction of information about protein-solvent interactions and molecular shape is also possible by means of multi-angle static light scattering measurements. In addition, light scattering is one of the suitable techniques for studying protein interaction/complexation with other proteins, ligands or biomacromolecules, as well as their aggregation in response to external stimuli like temperature, pH, ionic strength, etc.
Materials characterization infrastructure at the Theoretical and Physical Chemistry Institute (TPCI) of NHRF includes a Multi-Angle Static and Dynamic Light Scattering photometer CGS-3 Compact Goniometer System (ALV GmbH) with an Avalanche photodiode detector, interfaced with an ALV/LSE-5003 electronics unit and an ALV-5000/EPP multi-tau digital correlator. The system is equipped with a Polyscience model 9102 bath for temperature control, Glan-Thompson polarization prism and various types of cells. MALS selected services cover determination of protein molecular size and size distribution, hydrodynamic radius, average molecular weight, and radius of gyration. Moreover, information regarding the diffusion of the protein molecules, their shape and their interaction with the specific solvent are also available. Finally, studies on protein interactions and aggregation can also be performed.