Michael A. Kennedy
Eminent Scholar and Professor
Structural biology, structural genomics, DNA repair, NMR-based metabonomics, NMR spectroscopy, x-ray crystallography
My research involves the use of nuclear magnetic resonance spectroscopy (NMR) and x-ray crystallography to study the structure and function of proteins important to human health, host pathogen interactions, and novel metabolic pathways in exotic bacteria. We have particular interest in molecular mechanisms of human DNA repair, gene regulation in human adaptive immune responses, and NMR-based metabonomics to study several human diseases, including ovarian cancer and biliary atresia. My group is also part of a Large Scale Production Center for Structural Genomics funded by the National Institutes of Health’s Protein Structure Initiative whose goal is to make the three-dimensional structure of all proteins easily available from knowledge their amino acid sequences. Structural genomics requires high throughput protein structure determination using NMR and x-ray crystallography.
- T.A. Ramelot, J. R. Cort, S. Goldsmith-Fischman, G.J. Kornhaber, R. Xiao, R. Shastry, T. B. Acton, B. Honig, G.T. Montelione, and M.A. Kennedy “Solution NMR Structure of the Iron-Sulfur Cluster Assembly Protein U (IscU) with Zinc Bound at the Active Site” Journal of Molecular Bioliology, 344, 567-83, 2004.
- S. Ni, H. Robinson, C.G. Marsing, D.E. Bussiere, and M.A. Kennedy “Structure of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate Synthase from Shewanella oneidensis at 1.6Å: Identification of Farnesyl Diphosphate Trapped in a Hydrophobic Cavity” Acta Crystallographica Section D, 60,1949-57, 2004.
- G.W. Buchko, K. McAteer, S.S. Wallace, and M.A. Kennedy “Solution-State NMR Investigation of DNA Binding Interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): A Dynamic Description of the DNA /Protein Interface” DNA Repair, 4, 327-339, 2005.
- S. Ni, F. Farouhar, H. Robinson, D. E. Bussiere, and M.A. Kennedy (2005) "Structure Determination of VC0702 at 2.0Å, a Conserved Hypothetical Protein from Vibrio Cholerae” Proteins: Structure, Function, Bioinformatics, 63, 733-741, 2006.
- G.W. Buchko, S. Ni, H. Robinson, E. Welsh, H.Pakrasi, and M.A. Kennedy “Characterization of two potentially universal turn motifs that shape the repeated five residues fold- Crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142” Protein Science, 2006.
- T.A. Ramelot, A. Yee, J.R. Cort, A. Semesi, C.A. Arrowsmith, and M.A. Kennedy “NMR Structure and Binding Studies Confirm that PA4608 from Pseudomonas aeruginosa is a PilZ Domain and a c-di-GMP Binding Protein” Proteins: Structure, Function, and Bioinformatics, 2006.
- G.W. Buchko, Chang Y. Kim, Thomas C. Terwilliger, and Michael A. Kennedy “Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis” J. Bacteriology, 188, 5993-6001 (2006).