Upgrade of Bruker E500 EPR spectrometer
布鲁克E500 EPR光谱仪升级
基本信息
- 批准号:7794600
- 负责人:
- 金额:$ 50万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2010
- 资助国家:美国
- 起止时间:2010-02-04 至 2012-02-03
- 项目状态:已结题
- 来源:
- 关键词:BiologicalChemistryCrystallographyElectronsFunding ApplicantHousingMediatingMembraneMembrane FusionMembrane ProteinsMethodsMolecularPharmacologic SubstancePhysiologic pulsePhysiologyProteinsRecoveryResearchResolutionRunningSignal TransductionSiteSpin LabelsStructureSystemTechniquesTimeUniversitiesVirginiainstrumentmacromoleculeprotein complexresearch studytool
项目摘要
DESCRIPTION (provided by applicant): Funds are requested to upgrade an existing commercial Bruker Elexsys 500 continuous wave EPR spectrometer to add pulse capability. The upgraded instrument will be a highly versatile EPR instrument that will be capable of a broad range of pulse experiments with ns time resolution, but will retain the ability to run in CW mode. This instrument is also capable of saturation recovery as well as ELDOR experiments. This will be a multiuser instrument that will be housed and maintained by the Department of Chemistry. The primary user group will consist of five research groups at the University of Virginia: Profs. Bryant, Cafiso and Columbus in the Department of Chemistry, and Profs. Tamm and Nakamoto in the Department of Molecular Physiology. The facility will also be available to other research groups at the University. The primary use of the instrument will be for the determination of intermolecular distances within macromolecules using techniques such as double electron-electron resonance (DEER). A focus of the user group is to obtain information on the structure and dynamics of membrane proteins, and large protein complexes. This information will be used to determine the structures and structural changes in proteins that facilitate transport across biological membranes, the structures and mechanisms of proteins that facilitate membrane attachment in cell-signaling systems, and the mechanisms of protein- mediated membrane fusion. Membrane proteins are an extremely important class of proteins that are targets of the majority of the pharmaceuticals currently in use. Unfortunately, it is quite challenging to understand their molecular function, because they are not easily approached using standard structural methods such as crystallography and high-resolution NMR. As a result approaches using EPR, such as site-directed spin labeling, have become important tools to examine this class of proteins.
描述(由申请人提供):需要资金升级现有的商业Bruker Elexsys 500连续波EPR光谱仪,以增加脉冲能力。升级后的仪器将是一个高度通用的EPR仪器,将能够以ns时间分辨率进行广泛的脉冲实验,但将保留在CW模式下运行的能力。该仪器还可以进行饱和度恢复和Eldor实验。这将是一个多用户仪器,将由化学系安置和维护。主要用户组将由弗吉尼亚大学的五个研究小组组成:PRORS。Bryant,Cafiso和Columbus在化学系,以及教授。塔姆和中本聪在分子生理学系。该设施也将提供给该大学的其他研究小组。该仪器的主要用途将是使用双电子-电子共振(DER)等技术来确定大分子内的分子间距离。用户组的一个重点是获得关于膜蛋白和大型蛋白质复合体的结构和动力学的信息。这些信息将被用来确定促进生物膜运输的蛋白质的结构和结构变化,促进细胞信号系统中膜附着的蛋白质的结构和机制,以及蛋白质介导膜融合的机制。膜蛋白是一类极其重要的蛋白质,是目前使用的大多数药物的靶标。不幸的是,要了解它们的分子功能是很有挑战性的,因为它们不容易用标准的结构方法来研究,如结晶学和高分辨率核磁共振。因此,使用EPR的方法,如位点定向自旋标记,已经成为检测这类蛋白质的重要工具。
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)
数据更新时间:{{ journalArticles.updateTime }}
{{
item.title }}
{{ item.translation_title }}
- DOI:
{{ item.doi }} - 发表时间:
{{ item.publish_year }} - 期刊:
- 影响因子:{{ item.factor }}
- 作者:
{{ item.authors }} - 通讯作者:
{{ item.author }}
数据更新时间:{{ journalArticles.updateTime }}
{{ item.title }}
- 作者:
{{ item.author }}
数据更新时间:{{ monograph.updateTime }}
{{ item.title }}
- 作者:
{{ item.author }}
数据更新时间:{{ sciAawards.updateTime }}
{{ item.title }}
- 作者:
{{ item.author }}
数据更新时间:{{ conferencePapers.updateTime }}
{{ item.title }}
- 作者:
{{ item.author }}
数据更新时间:{{ patent.updateTime }}
DAVID S CAFISO其他文献
DAVID S CAFISO的其他文献
{{
item.title }}
{{ item.translation_title }}
- DOI:
{{ item.doi }} - 发表时间:
{{ item.publish_year }} - 期刊:
- 影响因子:{{ item.factor }}
- 作者:
{{ item.authors }} - 通讯作者:
{{ item.author }}
{{ truncateString('DAVID S CAFISO', 18)}}的其他基金
Molecular basis for the regulation of SNARE assembly in neuronal exocytosis
神经元胞吐作用中 SNARE 组装调节的分子基础
- 批准号:
10202630 - 财政年份:2005
- 资助金额:
$ 50万 - 项目类别:
MOLECULAR INTERACTIONS OF SYNAPTOTAGMIN MEDIATING MEMBRANE FUSION
突触结合蛋白介导膜融合的分子相互作用
- 批准号:
7036466 - 财政年份:2004
- 资助金额:
$ 50万 - 项目类别:
MOLECULAR BASIS FOR C2 DOMAIN-MEMBRANE INTERACTIONS
C2 域-膜相互作用的分子基础
- 批准号:
6691734 - 财政年份:2001
- 资助金额:
$ 50万 - 项目类别:
MOLECULAR BASIS FOR C2 DOMAIN-MEMBRANE INTERACTIONS
C2 域-膜相互作用的分子基础
- 批准号:
7048904 - 财政年份:2001
- 资助金额:
$ 50万 - 项目类别:
MOLECULAR BASIS FOR C2 DOMAIN-MEMBRANE INTERACTIONS
C2 域-膜相互作用的分子基础
- 批准号:
6228434 - 财政年份:2001
- 资助金额:
$ 50万 - 项目类别:
相似国自然基金
SCIENCE CHINA Chemistry
- 批准号:21224001
- 批准年份:2012
- 资助金额:24.0 万元
- 项目类别:专项基金项目
Science China Chemistry
- 批准号:21024801
- 批准年份:2010
- 资助金额:24.0 万元
- 项目类别:专项基金项目
运用Linkage Chemistry合成新型聚合物缀合物和刷形共聚物
- 批准号:20974058
- 批准年份:2009
- 资助金额:12.0 万元
- 项目类别:面上项目
相似海外基金
NMR crystallography: Imaging active site chemistry and protonation states
NMR 晶体学:对活性位点化学和质子化状态进行成像
- 批准号:
10406831 - 财政年份:2022
- 资助金额:
$ 50万 - 项目类别:
NMR crystallography: Imaging active site chemistry and protonation states
NMR 晶体学:对活性位点化学和质子化状态进行成像
- 批准号:
10673987 - 财政年份:2022
- 资助金额:
$ 50万 - 项目类别:
NMR crystallography: Imaging active site chemistry and protonation states
NMR 晶体学:对活性位点化学和质子化状态进行成像
- 批准号:
10797740 - 财政年份:2022
- 资助金额:
$ 50万 - 项目类别:
Engineering Enzymes for New Stereoselective and Stereodynamic Processes: An Integrated Chemistry -Bioengineering- X-Ray Crystallography-Molecular Dynamics Approach
用于新立体选择性和立体动力学过程的工程酶:化学-生物工程-X射线晶体学-分子动力学综合方法
- 批准号:
2023250 - 财政年份:2020
- 资助金额:
$ 50万 - 项目类别:
Standard Grant
Optimizing protein expression for X-ray crystallography studies and medicinal chemistry
优化 X 射线晶体学研究和药物化学的蛋白质表达
- 批准号:
552236-2020 - 财政年份:2020
- 资助金额:
$ 50万 - 项目类别:
University Undergraduate Student Research Awards
X-ray crystallography facilities for chemistry at Newcastle
纽卡斯尔化学 X 射线晶体学设施
- 批准号:
EP/F03637X/1 - 财政年份:2008
- 资助金额:
$ 50万 - 项目类别:
Research Grant
Crystallography and crystal chemistry of Fe-Al-Cu sulfates related to pollution created by acidic waters
与酸性水造成的污染相关的铁铝铜硫酸盐的晶体学和晶体化学
- 批准号:
19616273 - 财政年份:2006
- 资助金额:
$ 50万 - 项目类别:
Research Grants
Structural chemistry of inhibitor binding to Aldose Reductase: An integrated approach combining subatomic resolution crystallography, microcalorimetry, multipolar modeling and quantum modeling
抑制剂与醛糖还原酶结合的结构化学:结合亚原子分辨率晶体学、微量热法、多极建模和量子建模的综合方法
- 批准号:
5382941 - 财政年份:2002
- 资助金额:
$ 50万 - 项目类别:
Research Grants
Structural chemistry of inhibitor binding to Aldose Reductase: An integrated approach combining subatomic resolution crystallography, microcalorimetry, multipolar modeling and quantum modeling
抑制剂与醛糖还原酶结合的结构化学:结合亚原子分辨率晶体学、微量热法、多极建模和量子建模的综合方法
- 批准号:
5382933 - 财政年份:2002
- 资助金额:
$ 50万 - 项目类别:
Research Grants
Enhancement of Undergraduate Courses in Mineralogy, X-Ray Crystallography, Physical Chemistry, & Instrumental Analysiswith Improved X-Ray Diffraction Laboratory Experiences
矿物学、X射线晶体学、物理化学、
- 批准号:
9751355 - 财政年份:1997
- 资助金额:
$ 50万 - 项目类别:
Standard Grant