SMALL ANGLE SOLUTION X-RAY SCATTERING STUDIES ON METALLOPROTEINS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 基因组中超过一半的蛋白质含有金属，这些金属具有催化和/或结构作用。因此，它们在相当多的生理功能中发挥重要作用。该建议主要集中在可视化的构象和结构变化的（i）铜酶及其复合物的反硝化途径和（ii）蛋白质参与神经退行性疾病，由于其易感性聚集，在这里特别强调铜，锌超氧化物歧化酶。在没有任何结构信息的情况下，SAXS可以在低到中等分辨率下提供有价值的从头算3D形状。然而，我们的互补晶体学工作将使我们能够利用散射数据有意义的，特别是鉴于构象变化或协会的分子，其个别结构是已知的。

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. More than half of the proteins in a genome contain metals, which have catalytic and/or structural roles. They therefore play a significant part in a considerable number of physiological functions. This proposal primarily focuses on the visualization of conformations and structural changes of (i) Cu-enzymes and their complexes of the denitrification pathway and (ii) proteins involved in neurodegenerative diseases due to their susceptibility to aggregate, here with a particular emphasis on Cu, Zn superoxide dismutase. In the absence of any structural information SAXS can provide valuable ab initio 3D shapes at low to medium resolution. Yet our complementary crystallographic work will allow us to exploit the scattering data meaningfully in particular in view of conformational changes or associations of molecules whose individual structures are known.