The surfaces of mammalian cells are coated with complex carbohydrates, many terminated with a negatively charged "N"-acetylneuraminic acid residue. This motif is specifically targeted by pathogens, including influenza viruses and many pathogenic bacteria, to gain entry into the cell. A necessary step in the influenza virus life cycle is the release of viral particles from the cell surface; this is achieved by cleaving "N"-acetylneuraminic acid from cell surface glycans with a virally produced neuraminidase. We present a laboratory exercise to model this process using a glycoprotein as a glycan carrier and using real-time nuclear magnetic resonance spectroscopy to monitor "N"-acetylneuraminic acid release as catalyzed by neuraminidase. A time-resolved two-dimensional data-processing technique, statistical total correlation spectroscopy, enhances the resolution of the complicated one-dimensional glycoprotein spectrum and isolates characteristic peaks corresponding to substrates and products. This exercise is relatively straightforward and leads students through a wide range of biologically and chemically relevant procedures, including use of NMR spectroscopy, enzymology, and data-processing techniques. (Contains 5 figures.)