STRUCTURAL STUDIES OF GRAMICIDIN & OTHER SELF-ASSOCIATING PEPTIDES
短杆菌肽的结构研究
基本信息
- 批准号:7721416
- 负责人:
- 金额:$ 1.43万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2008
- 资助国家:美国
- 起止时间:2008-02-01 至 2009-01-31
- 项目状态:已结题
- 来源:
- 关键词:1-PropanolBehaviorBindingCell DeathComputer Retrieval of Information on Scientific Projects DatabaseDataFundingGasesGoalsGramicidinGrantHomoInstitutionIonsMass Spectrum AnalysisMembraneMetal Ion BindingMetalsMethodsPeptidesPhaseProteinsRangeReactionResearchResearch PersonnelResourcesSolutionsSolventsSourceTrifluoroethanolUnited States National Institutes of Healthdimermass spectrometermethod developmentmonomerself assemblysizetandem mass spectrometry
项目摘要
This subproject is one of many research subprojects utilizing the
resources provided by a Center grant funded by NIH/NCRR. The subproject and
investigator (PI) may have received primary funding from another NIH source,
and thus could be represented in other CRISP entries. The institution listed is
for the Center, which is not necessarily the institution for the investigator.
Our goal is to develop mass spectrometry combined with H/D exchange to study peptide and protein association reactions. Therefore, we chose gramicidin as the subject of our method development of MS methods to study the association of peptides and proteins in solution. Gramicidin is a membrane pentadecapeptide that acts as a channel, allowing the passage of monovalent metal ions and assisting in bacterial cell death. The active form is a noncovalently bound dimer. One means to study the self-assembly of this peptide has been to compare the state of the peptide in various solvents ranging from hydrophilic (e.g., trifluoroethanol) to hydrophobic (e.g., n-propanol). We are investigating the use of electrospray mass spectrometry to study the self-assocn. of gramicidin in various org. and mixed solvents that are introduced directly into the mass spectrometer. The dimer (both homo and hetero) can survive the introduction into the gas phase, and the amt. in the gas phase increases with the decreasing dielec. const. of the solvent, reflecting soln.-phase behavior. Tandem mass spectrometry data reveal that the stability of dimer in the gas phase decreases with increasing metal ion size, strongly suggesting that the metal ion binds inside the dimer between the monomers.
这个子项目是许多研究子项目中的一个
由NIH/NCRR资助的中心赠款提供的资源。子项目和
研究者(PI)可能从另一个NIH来源获得了主要资金,
因此可以在其他CRISP条目中表示。所列机构为
研究中心,而研究中心不一定是研究者所在的机构。
我们的目标是发展质谱结合H/D交换研究肽和蛋白质缔合反应。因此,我们选择短杆菌肽作为我们MS方法开发的主题,以研究溶液中肽和蛋白质的缔合。短杆菌肽是一种膜十五肽,作为通道,允许单价金属离子通过并协助细菌细胞死亡。 活性形式是非共价结合的二聚体。 研究这种肽的自组装的一种方法是比较肽在各种溶剂中的状态,从亲水性(例如,三氟乙醇)到疏水的(例如,正丙醇)。 我们正在研究使用电喷雾质谱来研究自缔合。将各种有机溶剂和混合溶剂中的短杆菌肽直接引入质谱仪。 二聚体(均聚体和杂聚体)可以在引入气相后继续存在,而amt。在气相中,随着扩散系数的减小而增加。溶剂的常数,反射溶液-相行为 串联质谱数据显示,二聚体在气相中的稳定性随着金属离子尺寸的增加而降低,强烈表明金属离子在单体之间的二聚体内部结合。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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MICHAEL L GROSS其他文献
MICHAEL L GROSS的其他文献
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{{ truncateString('MICHAEL L GROSS', 18)}}的其他基金
A Biomedical Mass Spectrometry Resource: Ongoing Driving Biomedical Projects
生物医学质谱资源:持续推动生物医学项目
- 批准号:
10441142 - 财政年份:2020
- 资助金额:
$ 1.43万 - 项目类别:
New chemical probes enable Mass Spectrometry-based footprinting of human protein structure in lipid membranes and cells
新的化学探针能够基于质谱分析脂膜和细胞中的人类蛋白质结构
- 批准号:
10350642 - 财政年份:2019
- 资助金额:
$ 1.43万 - 项目类别:
NEW CHEMICAL PROBES ENABLE MASS SPECTROMETRY-BASED FOOTPRINTING OF HUMAN PROTEIN STRUCTURE IN LIPID
新的化学探针实现了基于质谱的脂质中人类蛋白质结构的足迹
- 批准号:
10390166 - 财政年份:2019
- 资助金额:
$ 1.43万 - 项目类别:
NEW CHEMICAL PROBES ENABLE MASS SPECTROMETRY-BASED FOOTPRINTING OF HUMAN PROTEIN STRUCTURE IN LIPID MEMBRANES AND CELLS
新的化学探针能够对脂质膜和细胞中的人体蛋白质结构进行基于质谱的足迹分析
- 批准号:
10587527 - 财政年份:2019
- 资助金额:
$ 1.43万 - 项目类别:
APPROACHES TO IMPROVE PROTEIN FOOTPRINTING: HIGH PRESSURE DIGESTION
改善蛋白质足迹的方法:高压消化
- 批准号:
8361405 - 财政年份:2011
- 资助金额:
$ 1.43万 - 项目类别:
STRUCTURAL STUDIES OF GRAMICIDIN & OTHER SELF-ASSOCIATING PEPTIDES
短杆菌肽的结构研究
- 批准号:
8361321 - 财政年份:2011
- 资助金额:
$ 1.43万 - 项目类别:
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