STUDIES OF HSP169 OLIGOMERIZATION DOMAIN USING HYDROXYL RADICALS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Small Heat Shock Protein 16.9 reversibly oligomerizes from dimer to dodecamer upon heating. If a protein ligand unfolds at the higher temperature it stably binds to the dimer even upon cooling. A mutant of 16.9 only adopts the dimer state and cannot bind the protein ligand. Hydroxyl radicals have successfully demonstrated a change in oxidation upon transition to dimer:ligand association and clearly shows a difference in oxidation state between the 16.9 dodecamer and mutant dimer. We are proceeding to map the location of oxidation to determine the dodecamer interface.