Identifier

etd-06162005-144248

Degree

Master of Science (MS)

Department

Biological Sciences

Document Type

Thesis

Abstract

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.

Date

2005

Document Availability at the Time of Submission

Release the entire work immediately for access worldwide.

Committee Chair

Terry Bricker

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