IMPLICATIONS OF DISULFIDES BREAKING SEQUENCE IN REDUCTIVE UNFOLDING PATHWAYS

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。 利用我们为标准结晶学实验开发的在原子尺度上观察蛋白质晶体中随时间变化的结构的策略，通过对蛋白质的随时间变化的结晶学研究，观察到了由于X射线照射而导致的二硫键断裂的顺序。这些观察到的序列与蛋白质中的还原展开途径有关。目前的研究集中在牛胰腺核糖核酸酶A上，观察到的断裂序列正在与其他已建立的方法的结果进行比较。

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. The sequence of the breakage of disulfide bonds due to x-ray irradiation was observed by time-dependent crystallographic studies of proteins using the strategy we developed for time-dependent structure observations on the atomic scale in a protein crystal for standard crystallography experiments. These observed sequences are related to the reductive unfolding pathways in proteins. he current study focuses on bovine pancreatic ribonuclease A, where the observed breaking sequence is being compared to results by other established methods.