INTRINSICALLY DISORDERED PROTEINS AND MASS SPECTROMETRY

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。 蛋白质折叠、蛋白质动力学、蛋白质结构/功能关系、蛋白质-蛋白质相互作用和聚合/聚集机制是本实验室目前正在研究的项目。弗里登实验室特别感兴趣的是测量侧链堆积的动力学和折叠过程中的稳定性以及未折叠状态下的动力学。 他们还在研究固有无序蛋白质的动力学和聚集特性，包括AB、聚谷氨酰胺(单独和在Huntingtin Exon1中)和CsgA。CsgA是一种细菌蛋白，分泌到形成围绕细菌的纤维的介质中。研究包括通过变性剂展开的蛋白质的行为。这些方法主要有FCS法和核磁共振法(掺入氟标记氨基酸后)。

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. Protein folding, protein dynamics, protein structure/function relationships, protein-protein interactions and polymerization/aggregation mechanisms are projects currently under study in this laboratory. The Frieden laboratory is particularly interested in measuring the kinetics of side chain packing and stabilization during folding as well as dynamics in the unfolded state. They are also studying the dynamics and aggregation properties of intrinsically disordered proteins including AB, polyglutamine (alone and in huntingtin Exon1) and CsgA. CsgA is a bacterial protein secreted into the media forming fibrils that surround the bacteria. Studies include the behaviour of proteins unfolded by denaturant. The main methods for these sutdies include FCS and NMR (after incorporation of fluorine labeled amino acids).