NATIVE & RECOMBINANT MEMBRANE PROTEINS FOR DETERMINING FUNCTION MECHANISM

本国的

• 批准号: 7957382
• 负责人: CARLA L STORR
• 金额: $ 0.59万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-06-01 至 2010-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957382
• 关键词: 3-Dimensional; Antibody Formation; Biological Assay; Chemistry; Computer Retrieval of Information on Scientific Projects Database; Crystallization; Drug Design; Environment; Enzymes; Event; Family; Funding; G Protein-Coupled Receptor Genes; Grant; Institution; Integral Membrane Protein; Laboratories; Ligands; Mass Spectrum Analysis; Membrane Proteins; Peptides; Procedures; Process; Protein Biosynthesis; Proteins; RNA Processing; Recombinants; Research; Research Personnel; Resources; Signal Recognition Particle; Source; Structure; United States National Institutes of Health; design; enzyme substrate; member; polyketide synthase; receptor

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 laboratory focus is to reveal functional mechanisms of integral membrane proteins, soluble proteins, and peptides at the level of chemistry and atomic structure for impact on drug design. Membrane proteins include many members of the GPCR, TRP, Aquaglycerol, Vglut, and Amt families. Soluble proteins include RNA processing enzymes, SRP proteins, Polyketide Synthases, EPO receptors, and designed helical bundles. Synthesized peptides include those used for antibody production, enzyme substrates and ligands, and peptitergents. Following expression and synthesis, these proteins and peptides will be purified and characterized prior to 3-D crystallization. To facilitate characterization and crystallization, mass spectrometry will be used to assay purity, mass, and post-translational processing events. In addition, these efforts will further develop purification procedures of hydrophobic proteins and peptides in environments amenable for mass spectrometry.

该子项目是利用 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。 我们实验室的重点是揭示完整的膜蛋白，可溶性蛋白和肽在化学和原子结构水平上对药物设计的影响的功能机制。膜蛋白包括GPCR、TRP、Aquaglycerol、Vglut和Glycerol家族的许多成员。 可溶性蛋白质包括RNA加工酶、SRP蛋白、聚酮合酶、EPO受体和设计的螺旋束。 合成的肽包括用于抗体产生、酶底物和配体以及肽的那些。 在表达和合成之后，这些蛋白质和肽将在3-D结晶之前被纯化和表征。 为了便于表征和结晶，将使用质谱法测定纯度、质量和翻译后加工事件。此外，这些努力将进一步开发在适合质谱分析的环境中的疏水蛋白质和肽的纯化程序。