1B-O2-1700 PDF
Probing Structural Dynamics and Interactions of Intrinsically Disordered Proteins using Ion Mobility Combined with Mass Spectrometry
In this presentation, I will introduce applications of ion mobility mass spectrometry combined with other spectrometric/spectroscopic techniques for characterizing the conformational conversions and assembly mechanisms of proteins. Our laboratory has been focusing on understanding the structures dynamics of proteins in heterogeneous systems, such as lipid membranes and aqueous-organic co-solvent systems. Several examples of our studies related to probing dynamic equilibrium states of proteins will be presented. These studies elucidate the characteristic structures of proteins in various environments. For example, the secondary structures of α-synuclein, which is an amyloidogenic IDP, are changed by interactions with LUVs. ESI-IM-MS can distinguish and characterize different solution structures based on variances in the charge distributions and arrival time distributions of the protein ion in the gas phase. Utilizing this method, we also probed structural changes of other important amyloid proteins, such as β-amyloid and human islet amyloid polypeptide, in various environments. Implication of these observations to their functions and pathogenic pathways will be discussed.