Studying Lipoprotein Lipase oligomerization dynamics with cryoEM and mass photometry

Описание к видео Studying Lipoprotein Lipase oligomerization dynamics with cryoEM and mass photometry

In this webinar, you will learn how Dr. Kathryn Gunn and her colleagues from University of North Carolina at Chapel Hill, solved the structure of an active lipoprotein lipase (LPL) dimer and determined its oligomerization behaviours using cutting edge bioanalytical methods. You will discover how mass photometry can complement cryoEM data – determining the dynamic oligomerization states of LPL in solution, at varying concentrations and in the presence of additives. You will also learn how the air/water interface found in cryoEM samples can act as a substrate mimic. Taken together, the data will show how the diversity of LPL oligomerization may provide a form of regulation, influencing its activity in lipid metabolism and cardiovascular disease.

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