STRUCTURAL STUDIES ON PROTEINS, PEPTIDES AND ENZYMES OF IMPORTANCE IN BIONANOTEC

BIONANOTEC 中重要的蛋白质、肽和酶的结构研究

• 批准号: 8362183
• 负责人: KATHERINE A KANTARDJIEFF
• 金额: $ 0.36万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362183
• 关键词: 3-Dimensional; Alcohol Oxidoreductases; Biological Factors; California; Collection; Complex; Cysteine; Data; Data Collection; Drosophila melanogaster; Enzymes; Flavoproteins; Funding; Grant; Institution; Molecular; Molecular Chaperones; Myosin ATPase; NADPH Oxidoreductases NADH; National Center for Research Resources; Oxidoreductase; Peptides; Principal Investigator; Process; Proteins; RNA; Radiation; Recombinants; Research; Research Infrastructure; Resolution; Resources; Source; Sulfur; Time; United States National Institutes of Health; Universities; Yeasts; Zeolites; base; beta secretase; cost; cytochrome c; inhibitor/antagonist; mutant; nanobiotechnology; novel; protein structure; structural biology

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Research in the California State University and several predominantly undergraduate institutions involves the determination of the 3-D structures of proteins, peptides and enzymes of importance in bionanotechnology, biomedicine, environmental and industrial processes. This request for beam time at SSRL focuses on the collection of high resolution diffraction data from bacterial cytochromes c?, a novel myosin folding chaperone from Drosophila melanogaster, yeast carbonyl reductase mutants, single cysteine flavoprotein NAD(P)H oxidoreductases involved in sulfur reduction, a novel RNA safeguard enzyme TM0159 from Thermatoga maritima, recombinant beta-secretase in complex with natural product inhibitors, several dehydrogenases (complexes and mutants), and bio-zeolites based on helical peptides. The desire to collect data at SSRL is based upon our need for high quality, high resolution diffraction data from a number of different crystals, some of which are either too small or sensitive for conventional x-ray sources. While the majority of protein structures can be determined by molecular replacement, at least one requires accurate MAD data collection.

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 加州州立大学和几个主要的本科生机构的研究涉及确定在生物纳米技术、生物医学、环境和工业过程中重要的蛋白质、多肽和酶的三维结构。SSRL的束流时间要求集中在收集高分辨率的衍射数据，这些数据来自细菌细胞色素c？，一种新的果蝇肌球蛋白折叠伴侣蛋白，酵母羰基还原酶突变体，参与硫磺还原的单一半胱氨酸黄素蛋白NAD(P)H氧化还原酶，来自Thermatoga maritima的新的RNA保护酶TM0159，与天然产物抑制剂复合体中的重组β-分泌酶，几种脱氢酶(复合体和突变体)，以及基于螺旋肽的生物分子筛。在SSRL收集数据的愿望是基于我们对来自许多不同晶体的高质量、高分辨率衍射数据的需求，其中一些晶体对于传统的X射线源来说或者太小或者太敏感。虽然大多数蛋白质结构可以通过分子置换来确定，但至少有一个需要准确的MAD数据收集。