Original Broadcast Date: Wednesday May 4, 2016


Light scattering (LS), including classical and dynamic, has been widely employed to characterize protein solutions and other biomolecules. Classical or static light scattering, especially multi-angle light scattering (MALS), determines the absolute molecular weight of macromolecules in solution, facilitating the characterization of molecular heterogeneity and impurity profile. Dynamic light scattering (DLS), also known as quasi-elastic light scattering (QELS), directly measures the translational diffusion coefficient from which the hydrodynamic radius of a molecule is derived. Both static and dynamic light scattering can be used either in stand-alone (unfractionated, batch) mode or on-line coupled with a separation technique, such as size exclusion chromatography (SEC) or field-flow fractionation (FFF). In this seminar, application examples will be presented for simultaneously measuring molecular size of proteins and biomolecules using the DynaPro Plate Reader II. In addition, it will be discussed how to integrate DLS with MALS in a fractionation system and how the combined size and molar mass measurements can reveal unique insight into protein and biomolecule conformation and aggregation.

Learning Objectives:

  • Characterization of purified proteins and thermal stability over a range of solution conditions
  • Measuring the kinetics of macromolecular assemblies
  • Aggregate screening over several solution conditions, thermal conditions, and timeframes
  • Measuring the size and stability of liposome and virus particles
  • Crystallography screening of proteins over a range of solvent conditions

Presenter:
John Champagne, PhD
Senior Applications Scientist and Northeast Regional Manager
Wyatt Technology Corporation