Contact InformationOffice: WEL: 3.424
LabOffice: WEL 3.410
Jennifer S. Brodbeltjbrodbelt@cm.utexas.edu
William H. Wade Endowed Professor in Chemistry
Graduate Admissions Chair & Chemistry Graduate Advisor
Ph.D., Purdue University, 1988
B.S., University of Virginia, 1983
Postdoctoral Studies - University of California at Santa Barbara, 1989
Bioanalytical Mass Spectrometry
The Brodbelt group focuses on the development of ion trap mass spectrometry for a variety of interdisciplinary applications. Research efforts involve a number of aims: A) development of photodissociation methods for characterization of peptides, proteins, and lipids, B) exploration of derivatization methods to enhance the ionization and dissociation of molecules, C) design of new chemical probes to evaluate protein-ligand interactions.
Photodissociation for Analysis of Biological Molecules
Solving the most challenging biological problems requires advanced analytical strategies for characterizing complex mixtures of biomolecules. We are developing ultraviolet photodissociation methods to unravel the structures of biological molecules. UV photodissociation is a fast, high energy activation method, and it results in rich fragmentation patterns that serve as molecular fingerprints. This methodology is applied to elucidate the sequences and modifications of proteins as well as lipopolysaccharides that decorate the surfaces of bacteria.
Derivatization strategies provide the opportunity to modulate the chemical properties of molecules, ranging from hydrophobicity and basicity to volatility and ionizability. We are developing site-specific derivatization methods to attach charge sites and to append chromophores to molecules to control how peptides ionize and dissociate in the gas phase. UV photodissociation can be used to pinpoint chromophore-tagged molecules in complex mixtures and yield fragmentation patterns amenable to sequencing algorithms.
Determination of the correlation between protein structure and function remains a primary objective of biological research, thus motivating the development of advanced analytical tools for unraveling the three dimensional structures of proteins. We are developing an array of site-selective chemical probes that can be used to elucidate protein structure based on the accessibility or exposure of specific protein sites. This methodology is combined with photodissociation to provide detailed conformational maps of proteins.
Madsen, J., Boutz, D., Brodbelt, J.S., “Ultrafast Ultraviolet Photodissociation at 193 nm and its Applicability to Proteomic Workflows”, J. Proteome Research, 2010, 9, 4205-4214.
Madsen, J.A., Cullen, T.W., Trent, M.S., Brodbelt, J.S., “IR and UV Photodissociation as Analytical Tools for Characterizing Lipid A Structures”, Anal. Chem., 2011, 83, 5107-5113.
Vasicek, L., O’Brien, J.P., Browning, K.S., Tao, Z., Liu, H.W., Brodbelt, J.S., “Mapping Protein Surface Accessibility via an Electron Transfer Dissociation Selectively Cleavable Hydrazone Probe”, Mol. Cellular Proteomics, 2012, 11(7) 10.1074/mcp.O111.015826.
Robinson, M.R., Madsen, J.A., Brodbelt, J.S., “193 nm ultraviolet photodissociation of imidazolinylated lys-N peptides for de novo sequencing”, Anal. Chem., 2012, 84, 2433-2439.
Shaw, J., Ledvina, A., Zhang, X., Julian, R.R., Brodbelt, J.S., “Tyrosine Deprotonation Yields Abundant and Selective Back-bone Cleavage in Peptide Anions upon Negative Electron transfer Dissociation and Ultraviolet Photodissociation” J. Am. Chem. Soc., 2012, 134, 15624-15627.
Han, S-W., Lee, S-W., Bahar, O., Schwessinger, B., Robinson, MR., Shaw, J.B., Madsen, J.A., Brodbelt, J.S., Ronald, P.A., “Tyrosine sulfation in gram-negative bacterium”, Nature Commun., 2012, 3:1153 doi: 10.1038/ncomms2157.