SINGLE MOLECULE AND SAXS STUDIES OF EARLY COLLAPSE IN PROTEIN FOLDING

蛋白质折叠早期塌陷的单分子和 SAXS 研究

• 批准号: 8361284
• 负责人: Tobin R Sosnick
• 金额: $ 1.18万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-01-01 至 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361284
• 关键词: Biophysics; Contracts; Dimensions; Energy Transfer; Funding; Grant; Guanidinium Chloride; National Center for Research Resources; Principal Investigator; Proteins; Research; Research Infrastructure; Resources; Roentgen Rays; Source; Tertiary Protein Structure; United States National Institutes of Health; base; cost; protein folding; research study; single molecule

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Does the unfolded state contract at low-denaturant concentrations? Many single-molecule Forster Resonance Energy Transfer (sm-FRET) experiments suggest that unfolded, single domain proteins invariably collapse from random coil dimensions to a much more compact state as the denaturant concentration is reduced. However, the results of similarly numerous small angle X-ray scattering (SAXS) suggest instead that this effect may be rare. Here we explore this discrepancy via a detailed SAXS-based study of protein L, a protein that has been the subject of one previous SAXS study, which suggests the dimensions of the protein's unfolded state remain fixed between 6 and 1.4 guanidine hydrochloride (Gdm), and two prior sm-FRET studies, which suggest that the chain contracts by 20 to 30% over this same range.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 子项目的主要研究者可能是由其他来源提供的， 包括其他NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 未折叠的状态在低变性剂浓度下收缩吗？ 许多单分子福斯特共振能量转移（sm-FRET）的实验表明，未折叠的，单域蛋白质总是从随机卷曲尺寸崩溃到一个更紧凑的状态，因为变性剂浓度降低。然而，类似的许多小角X射线散射（SAXS）的结果表明，这种效应可能是罕见的。 在这里，我们通过一个详细的SAXS为基础的研究蛋白L，一个蛋白质，一直是一个以前的SAXS研究的主题，这表明蛋白质的未折叠状态的尺寸保持固定在6和1.4盐酸胍（Gdm）之间，和两个以前的sm-FRET研究，这表明，在这个相同的范围内，该链的合同由20%至30%，探索这种差异。