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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 不断增长的国家合同是否以低增生浓度？ 许多单分子福斯特共振能量转移（SM-FRET）实验表明，随着变性浓度降低，展开的单域蛋白总是从随机线圈尺寸崩溃到更紧凑的状态。但是，相似的众多小角X射线散射（SAX）的结果表明，这种效果可能很少见。 在这里，我们通过对蛋白L的详细研究探索这种差异，该蛋白质是一种先前的SAXS研究的主题，这表明该蛋白质展开状态的维度保持固定在6和1.4盐酸盐酸盐（GDM）（GDM）（GDM）之间，以及两项先前的SM-Fret研究，这表明该链条的研究表明，该研究表明，这表明连续合同相同20％，这是相同的链接合同。