Structural Information from Top-Down Tandem Mass Spectrometry of Protein Complexes

Analysis of protein complexes by ion mobility-mass spectrometry is a valuable method for the rapid assessment of complex composition, binding stoichiometries, and structures. However, capturing labile, unknown protein assemblies directly from cells remains a challenge for the technology. Furthermore, ion mobility-mass spectrometry measurements of complexes, subcomplexes, and subunits are necessary to build complete models of intact assemblies, and such data can be difficult to acquire in a comprehensive fashion. Our approach utilizes chemical modifications (in collaboration with Dr. Philip Andrews (UM Biological Chemistry) to stabilize intact complexes in the gas phase and promote formation of more compact product ions that better represent native protein subcomplexes.

Using chemical modifications to alter CID pathways to generate more structurally informative information from top-down tandem MS experiment.

 For more details, please refer to Samulak, B. M., et al., Anal. Chem., 2016, 88 (10).

For a detailed summary of current work in this research area, please visit the publication site.