A Proposal to expand analytical capabilities at Wayne State University with a 400
A Proposal to expand analytical capabilities at Wayne State University with a 400
批准号:
7595473
负责人:
PAUL M STEMMER
金额:
$50.0万
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
项目状态:
已结题
起止时间:
2009-05-01 至 2010-04-30
关键词:
AddressAreaArtsCellsCommitCore FacilityDiseaseFractionationFundingGoalsHybridsIonsLaboratoriesLipidsMaintenanceMeasuresMedicalOperative Surgical ProceduresPeptidesPhosphorylationPost-Translational Modification SitePost-Translational Protein ProcessingProcessProteinsProteomicsRelative (related person)ResearchResearch PersonnelSamplingScanningScheduleServicesSourceSystemTrainingUnited States National Institutes of HealthUniversitiesWagesbasebody systeminstrumentinstrumentationmass spectrometermeetingsmetropolitanmultiple reaction monitoringnanonoveloxidationprogramspublic health relevancesugar
中文摘要
描述(由申请人提供):本申请的目标是将应用生物系统4000 QTrap混合串联质谱仪与纳米LC一起应用于韦恩州立大学的蛋白质组学核心。该仪器具有独特的能力,可以利用三重四极杆能力发现翻译后修饰,并在仪器的线性离子陷阱组件中积累已识别的离子,以实现最高的灵敏度。这些功能的结合使4000 QTrap成为发现和定量的特殊仪器。4000个QTrap的可获得性和蛋白质组学核心中训练有素的操作员将是华盛顿州立大学NIH资助的研究人员研究计划的主要资产。该文书将解决目前没有得到充分满足的两个关键需求。第一个是发现蛋白质中新的翻译后修饰位点。第二种是从非常小的样本中定量测定蛋白质和修饰蛋白质。目前,韦恩州立大学或底特律大都市地区唯一可用于蛋白质组分析的MS/MS仪器是带有ETD的LTQ-XL,该仪器由寻求添加4000QTrap的同一蛋白质组学核心操作。LTQ被大量使用,不具备执行全光谱中性损耗扫描的能力,并且不是基于质量标签的定量或多反应监测的首选仪器。威斯康星州立大学EHS中心内的蛋白质组学设施核心已被确定为韦恩州立大学蛋白质组服务的唯一来源。该大学坚定地致力于这一申请,这证明了以下支持:1)Q Trap 4000的维护和运行的长期计划。2)翻新的蛋白质组学核心设施的实验室空间。3)为操作和安排仪器使用计划的技术人员的工资和培训提供资金。4000 QTrap混合串联质谱仪是一种最先进的系统,具有无与伦比的能力来检测和定位蛋白质的翻译后修饰,并对多肽进行相对和绝对定量。在华盛顿州立大学,这一仪器将允许更有效地使用已经到位的蛋白质组分离仪器,并将为NIH资助的研究人员提供高效的现代蛋白质组分析途径。与公共健康相关:我们的细胞、器官和系统受到蛋白质可逆变化的调节,如磷酸化、氧化和脂类或糖类的附着。了解疾病过程和验证医学治疗需要我们发现和测量蛋白质以及蛋白质的变化。4000 QTrap有效地搜索蛋白质修饰,并允许对蛋白质和修饰蛋白质进行灵敏的定量。
英文摘要
DESCRIPTION (provided by applicant): The goal of this application is to bring an Applied Biosystems 4000 QTrap hybrid tandem mass spectrometer with nano-LC to the Proteomics Core at Wayne State University. This instrument has unique capabilities for discovery of post translational modifications using the triple quadrupole capabilities and to accumulate identified ions in the linear ion trap component of the instrument for maximal sensitivity. The combined capabilities make the 4000 QTrap an exceptional instrument for both discovery and quantitation. The availability of the 4000 QTrap and a trained operator within the Proteomics Core will be a major asset to research programs of NIH-funded investigators at WSU. The instrument will address two critical needs that are currently not adequately met. The first of these is for the discovery of novel sites of post translational modification in proteins. The second is quantitation of proteins and modified proteins from very small samples. The only currently available MS/MS instrument at Wayne State University or in the metropolitan Detroit area that can be used for proteomic analysis is the LTQ-XL with ETD that is operated by the same Proteomics Core seeking to add the 4000QTrap. The LTQ is heavily used and does not have the capabilities to perform full spectrum neutral loss scans and is not the instrument of choice for mass tag based quantitation or multiple reaction monitoring. The Proteomics Facility Core within the EHS Center at WSU has been established as the only source for proteomic services at Wayne State. The University is strongly committed to this application as evidenced by the following support: 1) A long term plan for maintenance and operation of the Q Trap 4000. 2) Renovated laboratory space for the Proteomics Core Facility. 3) Funding for salary and training of a technician to operate and schedule usage of the instrument. The 4000 QTrap hybrid tandem mass spectrometer is a state-of-the-art system with unparalleled ability to detect and localize post-translational modifications in proteins and to perform both relative and absolute quantitation of peptides. At WSU, this instrument will allow more productive use of instrumentation already in place for proteomic fractionation and will provide efficient access to modern proteomic analysis for NIH- funded investigators. PUBLIC HEALTH RELEVANCE: Our cells, organs and systems are regulated by reversible changes in proteins such as phosphorylation, oxidation and the attachment of lipids or sugars. Understanding disease processes and validating medical therapies requires us to discover and measure the proteins and the changes in proteins. The 4000 QTrap efficiently searches for protein modifications and allows sensitive quantitation of proteins and modified proteins.
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会议论文
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