SAXS ANALYSIS OF NATIVELY UNFOLDED NUCLEOPORIN FG DOMAINS

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。列出的机构是 研究中心，而研究中心不一定是研究者所在的机构。 我们建议通过SAXS在不同温度下检查核孔蛋白（nups）的十个不同的天然未折叠结构域的三维形状，以确认和扩展我们的发现，即这些非结构化结构域中的一些采用在冷却时膨胀的紧凑构型（类似于原弹性蛋白），而另一些采用高度延伸的构型，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.