Research

Timeline of mass spec experiments

From our first experiments in 1993, in which we investigated protein folding pathways, through to our most recent investigations of membrane protein lipid interactions, mass spectrometry has played a central role. Not only have our experiments been able to uncover new insights into structure and function but have also motivated the development of instrumentation. The timeline above depicts major milestones in our journey. First, the transmission of the intact GroEL14-mer (aqua) in 1999 using instrumentation modified in our laboratory. Subsequently, we collaborated with others to develop ion mobility separations of ring-shaped and collapsed assemblies, and to produce early images of complexes on electron microscopy grids. Our first membrane protein complexes were ejected from micelles in 2008, and progressed to enable survival of intact rotary ATPases in 2011. Starting in 2014 we began our quest to uncover the many roles of lipids, starting with those that modulate the structure of membrane proteins, including the ammonia channel (upper rhs). In 2018, we recorded our first mass spectra of a G-protein coupled GPCR (lower rhs) with both endogenous ligand and drug retained. (Adapted with permission from https://doi.org/10.1073/pnas.1820450116)


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