What do we do?
The Molecular Profiling & Characterization Core characterizes the samples and is at the heart of our Center. Many of the measurements performed by the Core involve specialized mass spectrometers, and we have access to a wide range of instruments. Some of the instruments are located in the laboratories of Neil Kelleher at Northwestern University, while other measurement platforms are on the University of Illinois Urbana-Champaign campus, including an 11 T Fourier transform mass spectrometer, and an ion trap and several time-of-flight instruments, and two mass spectrometry imaging platforms. At Northwestern, Kelleher runs the Proteomics Center of Excellence with a range of high-end instruments available to the Center. These instruments and associated software enable high-performance protein identification and provide unmatched abilities to characterize post-translational modifications.
Due to the importance of determining signal molecule distribution in the brain, mass spectrometric imaging is also being developed using MALDI TOF/TOF technology. This analytical approach provides important clues about molecular function in biological systems, and dramatically eases analysis by uncovering specific brain regions that contain the highest levels of a protein, without requiring microdissection and isolation.
The Molecular Profiling & Characterization Core works closely with the Bioinformatics, Data Analytics and Predictive Modeling Core to increase the throughput and database search specificity of the raw data generated from diverse samples using the various mass spectrometers
Representative recent publications
Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (S)-3-Amino-(S)-4-fluorocyclopentenecarboxylic Acid, S. Shen, A. Butrin, B.A. Beaupre, G.M. Ferreira, P.F. Doubleday, D.H. Grass, W. Zhu, N.L. Kelleher, G.R. Moran, D. Liu, R.B Silverman, Molecules 28, 2023, 1133. DOI:10.3390/molecules28031133
Highly Multiplexed, Label-Free Proteoform Imaging of Tissues by Individual Ion Mass Spectrometry, P. Su, J.P. McGee, K.R. Durbin, M.A.R. Hollas, M. Yang, E.K. Neumann, J.L. Allen, B.S. Drown, F.A. Butun, J.B. Greer, B.P. Early, R.T. Fellers, J.M. Spraggins, J. Laskin, J.M. Camarillo, J.O. Kafader, N.L. Kelleher, Sci. Adv. 8, 2022, eabp9929. DOI:10.1126/sciadv.abp9929
ProSight Annotator: Complete Control and Customization of Protein Entries in UniProt XML Files, J.B. Greer, B.P. Early, K.R. Durbin, S.M. Patrie, P.M. Thomas, N.L. Kelleher, R.D. LeDuc, R.T. Fellers, Proteomics, 2022:e2100209. DOI:10.1002/pmic.202100209
Separation and Characterization of Endogenous Nucleosomes by Native Capillary Zone Electrophoresis-Top-Down Mass Spectrometry, K. Jooß, L. F. Schachner, R. Watson, Z.B. Gillespie, S.A. Howard, M.A. Cheek, M.J. Meiners, A. Sobh, J.D. Licht, M.C. Keogh, N.L. Kelleher, Anal. Chem. 93, 2021, 5151–5160. DOI:10.1021/acs.analchem.0c04975
Reassembling Protein Complexes After Controlled Disassembly by Top-Down Mass Spectrometry in Native Mode, L.F. Schachner, D.P. Tran, A. Lee, J.P. McGee, K. Jooss, K. Durbin, H. Dos Santos Seckler, L. Adams, E, Cline, R, Melani, A.N. Ives, B. Des Soye, N.L. Kelleher, S.M. Patrie, Int. J. Mass Spectrom. 465, 2021, 116591. DOI:10.1016/j.ijms.2021.116591