STUDIES OF HSP169 OLIGOMERIZATION DOMAIN USING HYDROXYL RADICALS

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心机构，不一定为研究者机构。小热休克蛋白16.9在加热时可逆地从二聚体寡聚为十二聚体。如果蛋白质配体在较高温度下解折叠，则其即使在冷却时也稳定地结合到二聚体。16.9的突变体仅采用二聚体状态并且不能结合蛋白质配体。羟基自由基已经成功地证明了在过渡到二聚体：配体缔合后氧化的变化，并且清楚地显示了16.9十二聚体和突变二聚体之间氧化态的差异。我们正在绘制氧化的位置，以确定十二聚体界面。

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.