Proteins

Proteins are the primary working molecules in all cells. However, many proteins can be altered through vairous covalent modification to fine tune their functions. Our work investigates the role of nitroso modifications in hemoglobin and the effects of covalent modficiation of proteins in cells by dietary quinone electrophiles. The objective of this project is to use mass spectrometry to characterize these covalent protein-ligand interactions.

• Stottlemeyer, Saylor; Cho, Tiffany; Plunkett, Ireland; Goring, Andrew; Scalzo, Fabien; Loo Joseph A.; Joyner, P. Matthew. Direct detection and characterization of S-nitrosohemoglobin using intact, native and top-down mass spectrometry. American Society for Mass Spectrometry Annual Meeting. Baltimore, MD (June 3, 2025)

• Hornback, Alyssa; Martinez Valdovinos, Abigail; Chang, Aracelli; Joyner, P. Matthew. Characterization of a cysteine-selective inhibitor of the bacterial fatty acid synthase enzyme enoyl-ACP reductase using mass spectrometry. American Chemical Society National Meeting and Exposition, Indianapolis, IN (March 25-30, 2023)

• Joyner, P. Matthew; Tran, Denise P. ; Zenaidee, Muhammad A.; Loo, Joseph A. Characterization of protein-ligand binding interactions of enoyl-ACP reductase (FabI) by native MS reveals allosteric effects of coenzymes and the inhibitor triclosan. Protein Science 2021, 31 (3), 568-579; https://doi.org/10.1002/pro.425

• Joyner, P. Matthew. Protein Adducts and Protein Oxidation as Molecular Mechanisms of Flavonoid Bioactivity. Molecules 2021, 26, 5102; https://doi.org/10.3390/molecules26165102