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This paper describes experiments that teach junior/senior undergraduate students about some of the uses of circular dichroism in characterizing several aspects of globular protein structure. The four experiments are (i) qualitative comparison of CD spectra for globular proteins with different amounts of secondary and tertiary structures, (ii) characterization of secondary and tertiary structure of the A state of cytochrome c, which is believed to resemble the molten globule, (iii) kinetics of lysozyme denaturation, and (iv) helicogenesis of concanavalin A, whereby the predominantly β-sheet protein structure is converted into mostly α-helix. These experiments have the pedagogical advantage of giving students experience with a spectroscopic method that provides more important details about protein structures than is provided by most routine spectroscopic methods.

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