CHROMOPHORE-CHROMOPHORE INTERACTIONS IN UNFOLDED LABELED PROTEINS/NATIVE COND

未折叠标记蛋白/天然条件中的发色团-发色团相互作用

• 批准号: 7601766
• 负责人: JACK JACOB
• 金额: $ 1.76万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-04-01 至 2008-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601766
• 关键词: Address; Biological Models; Computer Retrieval of Information on Scientific Projects Database; Condition; Conflict (Psychology); Dimensions; Fluorescence Resonance Energy Transfer; Funding; Grant; Institution; Investigation; Label; Measurement; Numbers; Proteins; Research; Research Personnel; Residual state; Resources; Source; Structure; Techniques; Time; United States National Institutes of Health; chromophore; design; nephelometry; polypeptide; protein folding; random coil (protein); research study; single-molecule FRET

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 commonly held view that unfolded proteins are random coils without any residual structure is being rigorously scrutinized currently. Some recent NMR studies have indicated that the unfolded state has a significant amount of residual structure that encodes the native topology. At the same time a number of small angle x-ray scattering (SAXS) and light scattering measurements have indicated that the average dimensions of the unfolded state correspond to that expected for random coils. Understanding the structure of the unfolded state is critical to many protein-folding studies. The unfolded state and partially unfolded intermediates have also been implicated in the aggregation of many proteins. There have been only relatively few SAXS studies on the unfolded state under native like conditions and our proposed experiments on two model systems are specifically designed to address this issue. Another conflicting issue that has emerged from investigations of the unfolded state is the discrepancy in results observed between SAXS and FRET measurements on a variety of different proteins. To further investigate this apparent discrepancy, which is critical to the interpretation of a multitude of ensemble and single molecule FRET studies, it would be extremely beneficial if both techniques were applied to a non-folding polypeptide with and without a FRET pair.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 人们普遍认为，未折叠的蛋白质是随机卷曲，没有任何残留结构，目前正在受到严格审查。最近的一些核磁共振研究表明，展开状态具有大量编码天然拓扑的残余结构。同时，许多小角度 X 射线散射 (SAXS) 和光散射测量表明，展开状态的平均尺寸与随机线圈的预期尺寸相对应。了解未折叠状态的结构对于许多蛋白质折叠研究至关重要。未折叠状态和部分未折叠中间体也与许多蛋白质的聚集有关。关于在类似自然条件下的展开状态的 SAXS 研究相对较少，我们提出的两个模型系统的实验是专门为解决这个问题而设计的。对未折叠状态的研究中出现的另一个相互矛盾的问题是对各种不同蛋白质进行 SAXS 和 FRET 测量时观察到的结果之间的差异。为了进一步研究这种明显的差异（这对于解释大量整体和单分子 FRET 研究至关重要），如果将两种技术应用于具有和不具有 FRET 对的非折叠多肽，将非常有益。