PULSED DIPOLAR ESR STUDY ON MEMBRANE-BOUND ALPHA-SYNUCLEIN

膜结合 α-突触核蛋白的脉冲偶极 ESR 研究

基本信息

  • 批准号:
    8364019
  • 负责人:
  • 金额:
    $ 0.45万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    2011
  • 资助国家:
    美国
  • 起止时间:
    2011-09-01 至 2012-08-31
  • 项目状态:
    已结题

项目摘要

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. The synaptic vesicle-associated protein, alpha-synuclein, is linked to both sporadic and familial Parkinson's disease through its appearance in Lewy bodies and through several genetic polymorphisms that lead to early onset of disease. Alpha-synuclein is intrinsically unstructured in solution, but it undergoes conformational changes to a predominantly ¿-helical structure upon association with lipid membranes. The functional conformation of this protein was shown to be the membrane bound form. Global fold of this protein was difficult to study by NMR because of luck in the proximis between subunits. Moreover, learning the structural aspect of protein-membrane interactions is not an easy task in general. The rapidly developing methods of NMR, such as TROSY, and pulsed dipolar ESR spectroscopy (PDS) are poised to address the challenges of measuring a wide range of distances ranging from a small fraction to tens or even hundreds of nanometers. Resent PDS study on ¿-synuclein elucidated in considerable details the structure of the protein in the context of detergent (SDS) and lyophospholipid micelles. It was shown that PDS provides high resolution and distances can be measured with a reasonable accuracy. This study reveals the presence of two membrane bound ¿-helices separated by a short linker. However, obtained data suggest the non-helical break between the helices may result from the spatial confinement of the micelle system.
这个子项目是利用这些资源的众多研究子项目之一

项目成果

期刊论文数量(0)
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科研奖励数量(0)
会议论文数量(0)
专利数量(0)

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ELKA R GEORGIEVA其他文献

ELKA R GEORGIEVA的其他文献

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{{ truncateString('ELKA R GEORGIEVA', 18)}}的其他基金

USE OF LIPIDIC NANODISCS FOR STRUCTURE/FUNCTION STUDIES ON MEMBRANE PROTEINS
使用脂质纳米圆盘进行膜蛋白的结构/功能研究
  • 批准号:
    8364070
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
FREEZE-QUENCH STUDY ON PROTEIN CONFORMATION STATE
蛋白质构象状态的冷冻淬灭研究
  • 批准号:
    8364073
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
PROBING ALPHA-SYNUCLEIN AGGREGATION
探测 α-突触核蛋白聚集
  • 批准号:
    8364109
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
PROBING BACTERIAL HOMOLOGUE OF GLUTAMATE TRANSPORTER BY PULSED DIPOLAR ESR
通过脉冲偶极 ESR 探测谷氨酸转运蛋白的细菌同源物
  • 批准号:
    8364071
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
NEW INSIGHTS INTO THE STRUCTURAL PROPERTIES OF ALPHA-SYNUCLEIN AND ITS MUTANTS
对 α-突触核蛋白及其突变体结构特性的新见解
  • 批准号:
    8364031
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
BUILDING UP THE FACILITY FOR MEMBRANE PROTEIN MANIPULATION AND SPIN LABELING
建立膜蛋白操作和旋转标记设施
  • 批准号:
    8364069
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
INCREASING THE DISTANCE RANGE AND RESOLUTION IN PULSED DIPOLAR ESR SPECTROSCOPY
提高脉冲偶极 ESR 光谱的距离范围和分辨率
  • 批准号:
    8364033
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
PULSED DIPOLAR ESR STUDY ON MEMBRANE OF EBOLA VIRUS FUSION PEPTIDE
埃博拉病毒融合肽膜的脉冲偶极ESR研究
  • 批准号:
    8364030
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
STRUCTURE DETERMINATION OF EBOLA VIRUS VP35 PROTEIN BY PDS
PDS 测定埃博拉病毒 VP35 蛋白的结构
  • 批准号:
    8364072
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:
PDS STUDY ON HUMAN PGP MDR TRANSPORTER ABCB1
人类 PGP MDR 转运蛋白 ABCB1 的 PDS 研究
  • 批准号:
    8364053
  • 财政年份:
    2011
  • 资助金额:
    $ 0.45万
  • 项目类别:

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