Acquisition of 700 MHz Wide-Bore NMR System for Solid-state NMR

获取用于固态 NMR 的 700 MHz 宽口径 NMR 系统

基本信息

  • 批准号:
    7498303
  • 负责人:
  • 金额:
    $ 200万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    2009
  • 资助国家:
    美国
  • 起止时间:
    2009-01-15 至 2013-07-14
  • 项目状态:
    已结题

项目摘要

DESCRIPTION (provided by applicant): Faculty of University of Illinois at Chicago (UIC), in collaboration with the major institutions in the Chicago area such as University of Chicago (UC) and the Argonne National Lab (Argonne) seek NIH funding to acquire a high-field wide-bore NMR system at a 1H frequency of 700 MHz or higher for development of new solid-state NMR (SSNMR) experiments on structural studies of biomolecules. The proposed purchase of an ultra-high- field SSNMR system responds to increasing demands and lack of ultra-high-field SSNMR instruments for biomolecular applications in the US. The proposed system also complements the UIC's existing ultra-high-field systems (800 MHz and 900 MHz) at the Center for Structural Biology in the medical center area because these narrow-bore systems equipped with cryoprobes are incapable of SSNMR experiments. The new spectrometer to be housed in an existing NMR room in the UIC Chemistry Department will be within a commuting distance (~30 min) from other Chicago-area institutions such as Argonne, UC, and Northwestern. Chicago's central location at a traffic hub of the Midwest also makes our site suitable for the unique ultra-high-field wide-bore NMR instrument dedicated for SSNMR in the Midwest. The new instrument will be will be a driving force of new interdisciplinary research and inter-institutional collaborations using SSNMR in this area. The new instrument will serve for our department members (150 graduate students, 20 postdoctral fellows, and 24 faculty) and other researchers (~50) in the Chicago-area institutes including UIC, UC, and, Argonne to perform advanced research in a number of areas including (a) structural biology of amyloid proteins and membrane proteins by SSNMR, (b) protein misfolding kinetics, (c) NMR and SSNMR characterization of novel natural products, organimetallics, and drugs, (d) drug metabolism, (e) membrane association of amyloid, (f) protein structures and dynamics of protein complexes, and (g) analysis of biomembrane bi-layer. In addition to the novel applications of NMR stated above, we will develop new SSNMR methods that would impact broad areas of medical and biological research. In particular, (1) we will develop novel methods to significantly enhance sensitivity in order to attain 10-fold time saving in SSNMR experiments for biomolecules and biomaterials. (2) We will offer new tools for structural analysis of amyloid proteins and membrane proteins, which have been major bottle necks in the current structural proteomics. PUBLIC HEALTH RELEVANCE: The impact of this proposal to the public health is two fold. First, our target includes amyloid proteins and membrane proteins, which are associated with various diseases; structural and functional studies proposed here will provide insights into the mechanisms of the diseases. Second, the state-of-the-art SSNMR instrument easily accessible to researchers in UIC and other Chicago-area institutions will generate excellent opportunities of research-based education on structural analysis of biomolecules by NMR and advanced NMR methods; undergraduate and graduate students will be uniquely trained as future work force in environments relevant to the public health.
描述(由申请人提供):伊利诺伊大学(UIC)的伊利诺伊大学教职生物分子。拟议购买超高现场SSNMR系统的需求不断增加,并且缺乏用于美国生物分子应用的超高现场SSNMR仪器。拟议的系统还补充了UIC在医疗中心地区结构生物学中心现有的UIC现有的超高场系统(800 MHz和900 MHz),因为这些配备有冷冻螺旋藻的狭窄孔系统无法接受SSNMR实验。在UIC化学部门现有的NMR房间中安置的新光谱仪将距离其他芝加哥地区机构(例如Argonne,UC和Northwestern)的通勤距离(约30分钟)。芝加哥位于中西部交通中心的中心位置也使我们的网站适合于中西部专用于SSNMR的独特的超高宽孔NMR仪器。新工具将是在该领域使用SSNMR进行新的跨学科研究和机构间合作的推动力。 The new instrument will serve for our department members (150 graduate students, 20 postdoctral fellows, and 24 faculty) and other researchers (~50) in the Chicago-area institutes including UIC, UC, and, Argonne to perform advanced research in a number of areas including (a) structural biology of amyloid proteins and membrane proteins by SSNMR, (b) protein misfolding kinetics, (c)新型天然产物,有机金和药物的NMR和SSNMR表征,(d)药物代谢,(e)淀粉样蛋白的膜关联,(f)蛋白质复合物的蛋白质结构和动力学,以及(g)生物膜双层的分析。除了上述NMR的新应用外,我们还将开发新的SSNMR方法,这些方法将影响医学和生物学研究的广泛领域。特别是(1)我们将开发新的方法来显着提高灵敏度,以便在生物分子和生物材料的SSNMR实验中节省10倍的时间。 (2)我们将提供用于淀粉样蛋白和膜蛋白的结构分析的新工具,这些蛋白质和膜蛋白在当前的结构蛋白质组学中一直是主要的瓶颈。公共卫生相关性:该提案对公共卫生的影响是两倍。首先,我们的靶标包括与各种疾病有关的淀粉样蛋白和膜蛋白。这里提出的结构和功能研究将提供有关疾病机制的见解。其次,UIC和其他芝加哥地区机构的研究人员很容易访问最先进的SSNMR仪器,将通过NMR和先进的NMR方法为基于研究的基于研究的教育提供了极好的机会;本科生和研究生将在与公共卫生相关的环境中作为未来的劳动力进行独特的培训。

项目成果

期刊论文数量(6)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
  • DOI:
    10.1039/c5cc04618a
  • 发表时间:
    2015-10-18
  • 期刊:
  • 影响因子:
    0
  • 作者:
    Wang S;Parthasarathy S;Xiao Y;Nishiyama Y;Long F;Matsuda I;Endo Y;Nemoto T;Yamauchi K;Asakura T;Takeda M;Terauchi T;Kainosho M;Ishii Y
  • 通讯作者:
    Ishii Y
Evolution of CPMAS under fast magic-angle-spinning at 100 kHz and beyond.
CPMAS 在 100 kHz 及以上快速魔角旋转下的演变。
  • DOI:
    10.1016/j.ssnmr.2015.10.002
  • 发表时间:
    2015
  • 期刊:
  • 影响因子:
    3.2
  • 作者:
    Wickramasinghe,Ayesha;Wang,Songlin;Matsuda,Isamu;Nishiyama,Yusuke;Nemoto,Takahiro;Endo,Yuki;Ishii,Yoshitaka
  • 通讯作者:
    Ishii,Yoshitaka
Nano-mole scale side-chain signal assignment by 1H-detected protein solid-state NMR by ultra-fast magic-angle spinning and stereo-array isotope labeling.
  • DOI:
    10.1371/journal.pone.0122714
  • 发表时间:
    2015
  • 期刊:
  • 影响因子:
    3.7
  • 作者:
    Wang S;Parthasarathy S;Nishiyama Y;Endo Y;Nemoto T;Yamauchi K;Asakura T;Takeda M;Terauchi T;Kainosho M;Ishii Y
  • 通讯作者:
    Ishii Y
Progress in proton-detected solid-state NMR (SSNMR): Super-fast 2D SSNMR collection for nano-mole-scale proteins.
Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning.
  • DOI:
    10.1021/ar4000482
  • 发表时间:
    2013-09-17
  • 期刊:
  • 影响因子:
    18.3
  • 作者:
    Parthasarathy, Sudhakar;Nishiyama, Yusuke;Ishii, Yoshitaka
  • 通讯作者:
    Ishii, Yoshitaka
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YOSHITAKA ISHII其他文献

YOSHITAKA ISHII的其他文献

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{{ truncateString('YOSHITAKA ISHII', 18)}}的其他基金

Structures and Toxicity of Amyloid Protein Assemblies in Alzheimer's
阿尔茨海默病中淀粉样蛋白组装体的结构和毒性
  • 批准号:
    8608544
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Structures and Toxicity of Amyloid Protein Assemblies in Alzheimer's
阿尔茨海默病中淀粉样蛋白组装体的结构和毒性
  • 批准号:
    8043940
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Structures and Propagation of Pathologically Relevant Amyloids in Alzheimer's
阿尔茨海默病中病理相关淀粉样蛋白的结构和传播
  • 批准号:
    9503822
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Molecular Structures and Kinetics of Amyloid Intermediates by Solid-State NMR
通过固态核磁共振研究淀粉样蛋白中间体的分子结构和动力学
  • 批准号:
    7624652
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Structures and Toxicity of Amyloid Protein Assemblies in Alzheimer's
阿尔茨海默病中淀粉样蛋白组装体的结构和毒性
  • 批准号:
    8416989
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Molecular Structures and Kinetics of Amyloid Intermediates by Solid-State NMR
通过固态核磁共振研究淀粉样蛋白中间体的分子结构和动力学
  • 批准号:
    7131493
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Structures and Toxicity of Amyloid Protein Assemblies in Alzheimer's
阿尔茨海默病中淀粉样蛋白组装体的结构和毒性
  • 批准号:
    8212240
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Molecular Structures and Kinetics of Amyloid Intermediates by Solid-State NMR
通过固态核磁共振研究淀粉样蛋白中间体的分子结构和动力学
  • 批准号:
    7278155
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Molecular Structures and Kinetics of Amyloid Intermediates by Solid-State NMR
通过固态核磁共振研究淀粉样蛋白中间体的分子结构和动力学
  • 批准号:
    7654343
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:
Structures and Propagation of Pathologically Relevant Amyloids in Alzheimer's
阿尔茨海默病中病理相关淀粉样蛋白的结构和传播
  • 批准号:
    9927626
  • 财政年份:
    2006
  • 资助金额:
    $ 200万
  • 项目类别:

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釉原蛋白丝带状组装体的淀粉样组装行为及其生物学功能特性研究
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