Investigations of Protein Folding by Solid State NMR

通过固态核磁共振研究蛋白质折叠

• 批准号: 8349713
• 负责人: ROBERT TYCKO
• 金额: $ 15.9万
• 依托单位: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/8349713
• 关键词: Address; Amyloid Fibrils; Biological Process; Chemicals; Collaborations; Computer Simulation; Crystallography; Data; Dependence; Development; Disease; Equilibrium; Freezing; Glass; Goals; Investigation; Kinetics; Label; Laboratories; Magic; Measurement; Measures; Methods; Modeling; Optics; Play; Process; Property; Proteins; Publishing; Relative (related person); Relaxation; Resolution; Role; Sampling; Site; Solutions; Solvents; Spectrum Analysis; Structural Models; Structure; System; Techniques; Technology; Thermodynamics; cold temperature; irradiation; microwave electromagnetic radiation; protein folding; research study; solid state nuclear magnetic resonance

No new protein folding experiments were performed in FY2011. However, much effort was devoted to the development of new solid state NMR technology that will enable experiments in FY2012, particularly a new low-temperature magic-angle spinning probe with microwave irradiation capabilities that will enhance the sensitivity of protein folding measurements by a factor of at least 50 relative to our previously published results. In addition, we have initiated a collaboration with Prof. Victor Munoz to measure and interpret solution NMR chemical shifts and relaxation parameters in thermally unfolded HP35, using isotopically labeled protein samples that were synthesized in our laboratory in FY2011 and previous years.

二零一一财政年度并无进行新的蛋白质折叠实验。 然而，大量的努力致力于开发新的固态NMR技术，这将使实验在2012财政年度，特别是一个新的低温魔角旋转探针与微波辐射能力，将提高蛋白质折叠测量的灵敏度至少50倍，相对于我们以前发表的结果。 此外，我们还与维克托穆尼奥斯教授合作，使用2011财年和前几年在我们实验室合成的同位素标记蛋白质样品，测量和解释热解折叠HP 35的溶液NMR化学位移和弛豫参数。

项目成果

What can solid state NMR contribute to our understanding of protein folding?

• DOI: 10.1016/j.bpc.2010.05.009
• 发表时间: 2010-09
• 期刊: BIOPHYSICAL CHEMISTRY
• 影响因子: 3.8
• 作者: Hu, Kan-Nian;Tycko, Robert
• 通讯作者: Tycko, Robert

Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.

• DOI: 10.1016/j.jmb.2009.07.073
• 发表时间: 2009-10-02
• 期刊: JOURNAL OF MOLECULAR BIOLOGY
• 影响因子: 5.6
• 作者: Hu, Kan-Nian;Havlin, Robert H.;Yau, Wai-Ming;Tycko, Robert
• 通讯作者: Tycko, Robert

Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance.

• DOI: 10.1021/ja908471n
• 发表时间: 2010-01-13
• 期刊: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
• 影响因子: 15
• 作者: Hu, Kan-Nian;Yau, Wai-Ming;Tycko, Robert
• 通讯作者: Tycko, Robert