DYNAMICS OF ELECTRON TRANSFER FLAVOPROTEIN

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。我们正在研究L7/L12结构域的全局和局部柔韧性，以确定该蛋白的溶液特性。结果将根据两个L7/L12结构域在完整核糖体中的位置和方向进行评估。此外，还将研究第二核糖体蛋白L10和延伸因子Tu与L7/L21的结合亲和力。这一数据将有助于我们进一步了解这些蛋白质在蛋白质延伸过程中如何在核糖体内合作。

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 global and local flexibility's of the L7/L12 domain are being investigated to identify the solution characterization of this protein. The results will be evaluated in terms of the position and orientation of the two L7/L12 domains in the complete ribosome. In addition, the postulant binding affinity of L10, a second ribosome protein, and elongation factor Tu with L7/L21 will be examined. This data should help further our understanding on how these proteins cooperate within the ribosome during a protein elongation.