Molecular parameters such as size, molar mass, and intermolecular interactions, which are important to identify and characterize intrinsically disordered proteins (IDPs), can be obtained from light scattering measurements. In this chapter, we discuss the physical basis of light scattering, experimental techniques, sample treatment, and data evaluation with special emphasis on studies on proteins. Static light scattering (SLS) is capable of measuring molar masses within the range 10(3)-10(8) g/mol and is therefore ideal for determining the state of association of proteins in solution. Since proteins are in general too small to obtain the geometric radius of gyration R (G) from SLS, it is more useful to determine the hydrodynamic Stokes radius, R (S), which can be obtained easily and quickly from dynamic light scattering (DLS) experiments. Accordingly, DLS is an appropriate technique to monitor expansion or compaction of protein molecules. This is especially important for IDPs, which can be recognized and characterized by comparing the measured Stokes radii with those calculated for particular reference states, such as the compactly folded and the fully unfolded states. The combined application of DLS and SLS improves measurements of the molar mass and is essential when changes in the molecular dimensions and molecular association/dissociation take place simultaneously.