SMALL ANGLE SOLUTION X-RAY SCATTERING STUDIES ON METALLOPROTEINS

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 基因组中超过一半的蛋白质含有金属，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扮演着重要的角色。这项建议主要集中在可视化的构象和结构的变化(I)铜酶及其复合体的反硝化途径和(Ii)参与神经退行性疾病的蛋白质由于其易聚性，这里特别强调铜，锌超氧化物歧化酶。在缺乏任何结构信息的情况下，SAXS可以在中低分辨率下提供有价值的从头算3D形状。然而，我们互补的结晶学工作将使我们能够有意义地利用散射数据，特别是考虑到其个别结构已知的分子的构象变化或缔合。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.