STUDIES OF HSP169 OLIGOMERIZATION DOMAIN USING HYDROXYL RADICALS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 小分子热休克蛋白16.9在受热时可逆地从二聚体寡聚为十二聚体。如果蛋白质配体在更高的温度下展开，它即使在冷却时也能稳定地与二聚体结合。16.9的突变体只处于二聚体状态，不能与蛋白质配体结合。羟基自由基已经成功地证明了在转变为二聚体时氧化的变化：配体缔合，并清楚地表明了16.9十二聚体和突变二聚体的氧化状态的不同。我们正在绘制氧化位置的地图，以确定十二聚体的界面。

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.