Michael C. Fitzgerald, Professor of Chemistry and Center for Biomolecular and Tissue Engineering

Contact Info:

Office Location:	3222 French Science Center
Office Phone:	(919) 660-1547
Email Address:
Web Page:	http://cbte.pratt.duke.edu/~mfitz

Education:

Ph.D.	University of Wisconsin, Madison	1994
B.S.	Davidson College	1989

Specialties:

Analytical
Biochemistry
Biomolecular Structure and Function

Research Interests:

Dr. Fitzgerald’s research group is focused on studies of protein folding and function. The group utilizes a combination of covalent labeling strategies (e.g. protein amide H/D exchange and methionine oxidiation) and mass spectrometry techniques to investigate the thermodynamic properties of protein folding and ligand binding reactions. Current research efforts involve: (1) the development new biophysical methods that enable protein folding and stability measurements to be performed on the proteomic scale; and (2) the application of these new methods in the areas of disease detection, diagnosis, and therapy.

Keywords:

Adenocarcinoma • Adult • Aged • Aged, 80 and over • Algorithms • Alleles • Amidines • Amino Acid Sequence • Amino Acid Substitution • Amino Acids • Animals • Anions • Antioxidants • Arginine • Automation • Bacterial Outer Membrane Proteins • Bacterial Proteins • Bacteriophage lambda • Base Sequence • bcl-X Protein • Binding Sites • Biological Markers • Biological Transport • Biophysical Phenomena • Biophysics • Blood Proteins • Buffers • Calcineurin • Calmodulin • Calorimetry • Carbonic Anhydrase II • Carcinoma, Non-Small-Cell Lung • Carrier Proteins • Catalysis • Cattle • Cell Line • Chromatography • Chromatography, Gel • Chromatography, High Pressure Liquid • Chromatography, Liquid • Circular Dichroism • Citrate (si)-Synthase • Coenzymes • Combinatorial Chemistry Techniques • Complex Mixtures • Copper • Cyclophilin A • Cyclosporine • Cytochromes c • Databases, Protein • Deuterium • Deuterium Exchange Measurement • Deuterium Oxide • Dimerization • Diterpenes • DNA • DNA-Binding Proteins • Dose-Response Relationship, Drug • Drug Discovery • Enzyme Activation • Enzyme Stability • Enzyme-Linked Immunosorbent Assay • Escherichia coli • Escherichia coli Proteins • Esters • Fatty Acid-Binding Proteins • Female • Ferric Compounds • Fluorescent Dyes • Fructose-Bisphosphate Aldolase • Fusarium • Gallium • Gene Expression Profiling • Genetic Complementation Test • Glutamate Dehydrogenase • Gonorrhea • Guanidine • Haemophilus influenzae • Heat-Shock Proteins • Histidine • Horses • Humans • Hydro-Lyases • Hydrogen • Hydrogen Bonding • Hydrogen Peroxide • Hydrogen-Ion Concentration • Hyperoxaluria, Primary • Immunoblotting • Immunohistochemistry • Immunosuppressive Agents • Indicators and Reagents • Iron • Iron-Binding Proteins • Isoelectric Focusing • Isomerases • Isotope Labeling • Kinetics • L-Lactate Dehydrogenase • Lactalbumin • Ligands • Lung Neoplasms • Lysine • Macrophage Migration-Inhibitory Factors • Malate Dehydrogenase • Male • Maltose • Maltose-Binding Proteins • Mass Spectrometry • Metalloproteins • Methionine • Mice • Microbial Sensitivity Tests • Microchemistry • Middle Aged • Models, Biological • Models, Chemical • Models, Molecular • Models, Theoretical • Molecular Chaperones • Molecular Sequence Data • Molecular Weight • Muser Mentor • Mutagenesis, Site-Directed • Mutation • Myoglobin • NAD • Neisseria gonorrhoeae • Neoplasms, Squamous Cell • Organometallic Compounds • Oxamic Acid • Oxidants • Oxidation-Reduction • Oxygen Isotopes • Peptide Biosynthesis • Peptide Fragments • Peptide Hydrolases • Peptide Mapping • Peptides • Peptostreptococcus • Periplasmic Binding Proteins • Pharmaceutical Preparations • Polymorphism, Genetic • Predictive Value of Tests • Prognosis • Protein Array Analysis • Protein Binding • Protein Conformation • Protein Denaturation • Protein Folding • Protein Footprinting • Protein Interaction Mapping • Protein Kinases • Protein Stability • Protein Structure, Secondary • Protein Structure, Tertiary • Protein Subunits • Proteins • Proteome • Proteomics • Protons • Pteridines • Pyridoxal Phosphate • Pyrones • Quantum Theory • Rabbits • Recombinant Fusion Proteins • Recombinant Proteins • Repressor Proteins • Reproducibility of Results • Ribonuclease, Pancreatic • Ribonucleases • Saccharomyces cerevisiae • Saccharomyces cerevisiae Proteins • Sensitivity and Specificity • Sequence Homology, Amino Acid • Small Molecule Libraries • Sorbic Acid • Spectrometry, Fluorescence • Spectrometry, Mass, Electrospray Ionization • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization • Spectrophotometry • Spectrophotometry, Ultraviolet • src Homology Domains • Stereoisomerism • Stilbenes • Streptococcus • Structure-Activity Relationship • Substrate Specificity • Sulfonium Compounds • Sulfurtransferases • Superoxide Dismutase • Survival Analysis • Swine • Tandem Mass Spectrometry • Temperature • Thermodynamics • Time • Time Factors • Transaminases • Transcription Factors • Transferrin • Transferrin-Binding Protein A • Transferrin-Binding Protein B • Trypsin • Tumor Markers, Biological • Ubiquitin • UDPglucose 4-Epimerase • Ultraviolet Rays • Urea • Variation • Viral Proteins • Viral Regulatory and Accessory Proteins • Vitamin B Complex • Yeasts

Current Ph.D. Students   (Former Students)

• Fang Liu  
• Ryenne Ogburn  
• Julia Roberts  
• Xiaopu (Lorrain) Jin  
• Ariel Greer  
• Jagat Adhikari  
• Erin Hopper  
• Tabitha George  
• Petra Roulhac  
• Liyuan Ma  
• Graham West  
• Liangjie Tang  

Postdocs Mentored

• Victor Anbalagan (2007 - 2010)  

Recent Publications   (More Publications)

1. Gurysh, EG; Zahid, MSH; Johnson, MM; Landavazo, A; Namjoshi, OA; Wilson, JW; Varma, DM; Woodring, RN; Hendricksen, AT; Vath, JF; Quan, B; Pino, EN; Fitzgerald, MC; Bachelder, EM; Blough, BE; Ainslie, KM, Discovery of Host-Directed Small Molecules with Broad Anti-Leishmanial Efficacy., bioRxiv (November, 2025) [doi]  [abs]
2. Denning-Jannace, CA; James, KJ; Monteagudo, CR; Sturrock, GR; Robison, ATR; Vaccaro, FA; Kuhn, SA; Fitzgerald, MC; Franz, KJ, Leveraging Vulnerabilities in Copper Trafficking for Synergistic Antifungal Activity., ACS chemical biology, vol. 20 no. 11 (November, 2025), pp. 2659-2670 [doi]  [abs]
3. Outlaw, TC; Robison, ATR; Schulte, NB; Vaccaro, FA; Williams, IG; Repala, S; Diaz, D; Sturrock, GR; Fitzgerald, MC; Franz, KJ, Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase., Biochemistry, vol. 64 no. 21 (November, 2025), pp. 4400-4413 [doi]  [abs]
4. Truong, A; Hu, R; Quan, B; Bailey, MA; Schroeder, EA; Sylvester, K; Neveu, G; Kafsack, BFC; Fitzgerald, MC; Derbyshire, ER, Covalent inhibition of <i>Plasmodium falciparum</i> Ubc13 impairs global protein synthesis., iScience, vol. 28 no. 6 (June, 2025), pp. 112545 [doi]  [abs]
5. Sturrock, GR; Robison, ATR; Dharani, A; Monson, EE; Franz, KJ; Fitzgerald, MC, Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes., Protein science : a publication of the Protein Society, vol. 34 no. 6 (June, 2025), pp. e70158 [doi]  [abs]