Identification of peptide epimers in crystallin proteins
晶状体蛋白中肽差向异构体的鉴定
基本信息
- 批准号:8901229
- 负责人:
- 金额:$ 26.75万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2014
- 资助国家:美国
- 起止时间:2014-08-01 至 2018-07-31
- 项目状态:已结题
- 来源:
- 关键词:AcidsAffectAgeAge-YearsAgingAlzheimer&aposs DiseaseAmino AcidsAspartic AcidAutomationBlindnessCataractCollagenCrystallinsCysteineData AnalysesDentinDevelopmentDiseaseDissociationEye Lens ProteinFundingGeneric DrugsGoalsHandednessHealthHumanIndividualIsoaspartic AcidIsomerismLeadLifeManualsMass Spectrum AnalysisMethodsModificationMolecularMolecular ChaperonesMotivationMyopathyOutcomeOxidative StressPathologyPeptidesPerformancePlayPost-Translational Protein ProcessingProteinsProteomicsProtocols documentationResearchResolutionRoleSamplingSiteStructureTechniquesUnited States National Institutes of HealthWorkbasecostdisulfide bondepimerizationextreme temperatureimprovedinnovationinsightinstrumentinterestlensmass spectrometermigrationpreventprogramsprotein aggregationprotein degradationprotein structureracemizationresearch studyscale uptool
项目摘要
DESCRIPTION (provided by applicant): The overall goal of this project is to employ an innovative mass spectrometric technique to detect and characterize modifications to the chirality of individual amino acids within peptides and proteins. Chirality, or the handedness of a molecule, is a crucial attribute that influences both structure and function. Changes in chirality are very difficult to detect; however, a new method dependent on site specific radical migration is extremely sensitive to structure and can detect changes in chirality. The underlying motivation for performing this research is to investigate potential causes of cataract disease and to understand how protein modifications influence aging in general. Changes in chirality have been examined in primarily a generic sense in eye lens proteins previously, and these changes have been noted to increase for cataractous lenses. Site-specific examination of changes in chirality has not been carried out previously because no suitable tool was available for performing the task. The outcome of this project will be detailed information that elucidates how chiral inversion
contributes to cataract formation and to aging in general, which is necessary to guide the development of potential preventative treatments.
描述(由申请人提供):该项目的总体目标是采用创新的质谱技术来检测和表征肽和蛋白质内单个氨基酸的手性修饰。手性或分子的旋向性是影响结构和功能的关键属性。手性的变化很难被检测到;然而,一种依赖于位点特异性自由基迁移的新方法对结构极其敏感,并且可以检测手性的变化。进行这项研究的根本动机是调查白内障疾病的潜在原因,并了解蛋白质修饰如何影响衰老。此前,人们主要在一般意义上对眼晶状体蛋白的手性变化进行了研究,并且已经注意到这些变化对于白内障晶状体来说会增加。之前尚未对手性变化进行现场特定检查,因为没有合适的工具可用于执行该任务。该项目的成果将是阐明手性反转如何进行的详细信息
一般而言,它会导致白内障的形成和衰老,这对于指导潜在预防治疗的开发是必要的。
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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Ryan Roy Julian其他文献
Ryan Roy Julian的其他文献
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{{ truncateString('Ryan Roy Julian', 18)}}的其他基金
Connecting long-lived protein isomerization to lysosomal failure in Alzheimer's disease
将长寿命蛋白质异构化与阿尔茨海默氏病溶酶体衰竭联系起来
- 批准号:
10377485 - 财政年份:2020
- 资助金额:
$ 26.75万 - 项目类别:
Connecting long-lived protein isomerization to lysosomal failure in Alzheimer's disease
将长寿命蛋白质异构化与阿尔茨海默氏病溶酶体衰竭联系起来
- 批准号:
10600990 - 财政年份:2020
- 资助金额:
$ 26.75万 - 项目类别:
Identification of peptide epimers in crystallin proteins
晶状体蛋白中肽差向异构体的鉴定
- 批准号:
9306129 - 财政年份:2014
- 资助金额:
$ 26.75万 - 项目类别:
Rapid ultra-sensitive three dimensional protein structure determination by mass s
通过质量数快速测定超灵敏三维蛋白质结构
- 批准号:
8319335 - 财政年份:2011
- 资助金额:
$ 26.75万 - 项目类别:
Rapid ultra-sensitive three dimensional protein structure determination by mass s
通过质量数快速测定超灵敏三维蛋白质结构
- 批准号:
8164717 - 财政年份:2011
- 资助金额:
$ 26.75万 - 项目类别:
Rapid ultra-sensitive three dimensional protein structure determination by mass s
通过质量数快速测定超灵敏三维蛋白质结构
- 批准号:
8510672 - 财政年份:2011
- 资助金额:
$ 26.75万 - 项目类别:
Probing Natively Disordered Proteins with Selective Noncovalent Adduct Protein Pr
用选择性非共价加合物蛋白 Pr 探测天然无序蛋白
- 批准号:
7945317 - 财政年份:2009
- 资助金额:
$ 26.75万 - 项目类别:
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