To study conformational changes in myoglobin, two techniques can be used: fluorescence spectroscopy and circular dichroism spectroscopy.

Fluorescence Spectroscopy:
- Fluorescence spectroscopy is a technique that measures the emission of light from a molecule after it has absorbed light of a specific wavelength.
- Myoglobin contains a heme group that can absorb light and emit fluorescence.
- By monitoring the fluorescence emission of myoglobin at different wavelengths, it is possible to study conformational changes in the protein.
- Changes in the fluorescence emission spectrum can indicate changes in the environment of the fluorophore, which can result from conformational changes in the protein structure.
- This technique is useful for studying structural changes in myoglobin, as changes in the protein conformation can affect the accessibility and environment of the fluorophore, leading to changes in fluorescence emission.

Circular Dichroism Spectroscopy:
- Circular dichroism spectroscopy is a technique that measures the differential absorption of left- and right-circularly polarized light by chiral molecules.
- Myoglobin is a chiral protein, meaning it has a specific handedness or asymmetry in its structure.
- By measuring the differential absorption of circularly polarized light by myoglobin, it is possible to obtain information about its secondary structure and conformational changes.
- Circular dichroism spectroscopy can provide information about changes in the protein's secondary structure, such as the alpha-helix and beta-sheet content, which can be indicative of conformational changes.
- This technique is particularly useful for studying changes in the protein secondary structure, which can occur during conformational changes.

In summary, fluorescence spectroscopy and circular dichroism spectroscopy are both useful techniques for studying conformational changes in myoglobin. Fluorescence spectroscopy can provide information about changes in the environment of the fluorophore, while circular dichroism spectroscopy can provide information about changes in the protein's secondary structure. Using both techniques together can provide complementary information about conformational changes in myoglobin.