Nanodiscs, Membrane Proteins, and Mass Spectrometry: New Tools for Studying Protein-Lipid Interaction
Dr. Michael Marty, '10
Friday September 26th, 3:15, Regents 310
Membrane proteins play a critical role in biochemistry, bioenergy, and pharmaceuticals. However,
little is known about interactions between membrane proteins and their lipid bilayer environment.
This is largely due to a lack of adequate tools for quantifying these complex interactions. Nanodiscs,
nanoscale lipoprotein particles modeled after HDL, provide a unique platform for studying
membrane proteins in a homogeneous and monodisperse lipid bilayer environment. I will present
research examining membrane proteins embedded in Nanodiscs with native ion mobility-mass
spectrometry. Native mass spectrometry preserves noncovalent interactions, allowing detection
of the intact membrane protein-Nanodisc complex as well as metastable dissociation products.
Comparing the masses of these dissociation products with molecular dynamics simulations
reveals a “magic number” of lipids that corresponds to the number of polar contacts between
the membrane protein and its lipid bilayer annular belt. This combination of nanotechnology,
biochemistry, and mass spectrometry provides new tools for quantifying interactions between the
lipid bilayer and membrane proteins.
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