Progressing protein mass spectrometry closer to the physiological milieu
Dr Mark Agasid
Department of Chemistry, University of Oxford
Time & Place
Wed, 19 Feb 2020 12:00:00 NZDT in Room 031 Jack Erskine Building
All are welcome
The biological environments of proteins are composed of complex chemical matrices consisting of ions, small-molecules, peptides, and other proteins. This dynamically changing landscape is also critically important for protein structure and function. Over the past 25 years, mass spectrometry of intact proteins and protein complexes has elucidated important details of protein-ligand and protein-protein interactions, owing to high mass accuracy and resolution. However, the millimolar concentrations of non-volatile salts present in physiological solutions have posed a significant challenge in studying these macromolecular assemblies in their native solution conditions. Here, I describe advancements in the electrospray ionisation of soluble and membrane proteins from high-salt environments and how this may be coupled to improvements in mass spec instrumentation to garner greater details about protein assemblies.
Mark graduated from the University of California San Diego and completed his PhD studies at the University of Arizona. He joined the Professor Dame Carol Robinson research group in 2017.