Chromatography: Protein Purification

This lecture covers the principles of chromatography for protein purification, focusing on columns and the resolution of chromatography. It explains the causes of peak broadening, such as eddy diffusion, mobile phase mass transfer, and stagnant mobile phase mass transfer. The lecture also discusses the physical components of band broadening and the van Deemter curve. Different chromatography components, including refractive index, viscosity, light scattering, and absorbance, are analyzed using a tetra detector array. Commonly used stationary phases and gel filtration media are presented, along with the principles of ion exchange chromatography and immobilized metal affinity chromatography.