Lecture
Chromatography: Protein Purification
In course
DEMO: incididunt nostrud elit
Sunt voluptate commodo nisi commodo ex esse aliqua commodo ex ad Lorem ea quis. Ut minim ut mollit quis culpa reprehenderit fugiat. Eiusmod pariatur ea nulla ullamco consequat in veniam. Minim consequat mollit ipsum ex labore dolore. Dolor excepteur ad ex quis.
Description
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.
Instructor
deserunt duis
Consectetur irure ex ullamco ut. Quis labore minim esse anim dolor. Veniam ex in magna proident occaecat in dolore sit est.
Official source
About this result
This page is automatically generated and may contain information that is not correct, complete, up-to-date, or relevant to your search query. The same applies to every other page on this website. Please make sure to verify the information with EPFL's official sources.
Related lectures (46)
Protein Mass Spectrometry and Proteomics: Techniques and Applications
Explores protein mass spectrometry techniques, including labeling methods, quantitation, and biomarker discovery.
Protein Mass Spectrometry and Proteomics
Covers the fundamentals of protein mass spectrometry and proteomics, including chromatography techniques, efficiency, resolution, and peptide IEF applications.
Protein Mass Spectrometry and Proteomics
Explores liquid chromatography principles, various chromatographic techniques, HPLC components, and the comparison between off-gel IEF and SCX chromatography.
Exploring Proteins: Structure, Purification, and Analysis
Covers protein exploration, purification, and analysis methods, including sequencing, concentration measurement, and antibody detection.
Protein Mass Spectrometry and Proteomics
Explores protein mass spectrometry, chromatographic techniques, and quantitative proteomic workflows, including SILAC and isobaric tagging methods.