Conformational changes in the extrinsic manganese stabilizing protein can occur upon binding to the photosystem II reaction center: an isotope editing and FT-IR study

Isotope editing and Fourier-transform infrared spectroscopy were used to elucidate the changes that take place in manganese stabilizing protein (MSP) upon functional reconstitution to photosystem II. The results showed consistency in the major conformational changes, with around 30 to 40% of the peptide structure exhibiting a change in secondary structure. The findings provided strong evidence that folding of MSP can be caused by the binding of MSP to the reaction center and that MSP can have a wide array of conformational states.