SAXS ANALYSIS OF NATIVELY UNFOLDED NUCLEOPORIN FG DOMAINS

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。 我们建议用SAXS研究10个不同天然展开的核孔蛋白(NUP)结构域在不同温度下的三维形状，以证实和扩展我们的发现，其中一些非结构域采用致密的构型(类似于原弹性蛋白)，而另一些则采用高度伸展的构型，这取决于它们的氨基酸组成。

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. We propose to examine the three-dimensional shape of ten different natively- unfolded domains of nucleoporins (nups) by SAXS at different temperatures to confirm and extend our findings that some of these unstructured domains adopt compact configurations that swell upon chilling (similar to tropoelastin), while others adopt highly-extended configurations, depending on their amino acid composition.