Master of Science (MS)


Biological Sciences

Document Type



The structural association of the spinach 17 kDa protein of photosystem II with other extrinsic and membrane-bound components of the photosystem was investigated by labeling the 17 kDa protein with the amino group-specific reagent N-hydrosuccinimidobiotin both on intact photosystem II membranes and free in solution. Following isolation of the biotinylated molecules, the modified 17 kDa protein was allowed to rebind at various molar ratios to photosystem II membranes lacking the 17 kDa protein. Differential binding of the biotinylated proteins compared to unmodified 17 kDa protein indicates steric or ionic interference due to added biotin moieties, impeding physical contact or shielding positively charged amino groups, respectively. Biotinylated sites on the different modified 17 kDa proteins were identified by trypsin and Staphylococcus V8 protease digestion, followed by affinity chromatography enrichment for biotinylated molecules, and analysis of the resultant peptide fragment mixture by nanospray LC mass spectrometry. Areas shielded from the bulk solvent when the protein is associated with photosystem II may correspond to protein segments involved in the interaction with other components of the photosystem.



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Committee Chair

Terry Bricker