INTRINSICALLY DISORDERED PROTEINS AND MASS SPECTROMETRY

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。子项目及 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。所列机构为 研究中心，而研究中心不一定是研究者的研究机构。 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。Frieden实验室特别感兴趣的是测量折叠过程中侧链包装和稳定的动力学以及未折叠状态下的动力学。 他们还研究了内在无序蛋白质的动力学和聚集特性，包括AB，聚谷氨酰胺（单独和亨廷顿外显子1）和CsgA。CsgA是分泌到培养基中形成包围细菌的原纤维的细菌蛋白。研究包括变性剂解折叠的蛋白质的行为。这些研究的主要方法包括FCS和NMR（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).