Scientist must look beyond studying individual proteins and examine the structure and assembly of protein complexes within cells in order to truly understand how proteins function in their native environment. The emergence of cryo-electron microscopy (cryo-EM) has resulted in the ability to directly visualize complete macromolecular complexes in near-atomic level resolution. Combined with advances in mass spectrometry (MS), these methods have had a considerable impact on structural biology research, enabling researchers to characterize biomolecular structures with greater speed, sensitivity and selectivity. Dr. Pascal Albanese discuss the characterization of a key enzyme of the central carbon metabolism of Pyrococcus furious, through an integrative approach combining structural mass spectrometry, cryo-electron microscopy, mass photometry and molecular modelling with molecular dynamics simulations. He will describe how his lab unveiled the structural organization of phosphoenolpyruvate synthase (PPSA).

 

Learning Objectives