Ion mobility mass spectrometry insights into dynamic protein complexes and conformations

Research into the structure-function relationship of proteins has been a productive area of study over many decades, contributing to our understanding of biology and health and hence to the development of therapies. Whilst many methods are able to predict structures of proteins that exist in a single conformation, investigating proteins that exist in multiple shapes and stoichiometries remains challenging. Ion mobility mass spectrometry (IMMS) can report on the size range of every species that is present in a stoichiometric mixture, including co-existing conformations of the same species, without any time or ensemble averaging. 

In this presentation I will demonstrate that IMMS is particularly suitable for investigating intrinsically disordered proteins (IDPs) that exist and function in a wide range of conformations. I will describe how IMMS can track the conformations of IDPs that are responsible for liquid-liquid phase separation, as well as delineate their conformational change in response to drug and ligand binding. 

Find out more about Dr Rebecca Beveridge