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: 7722160
• 负责人: KATHERINE A KANTARDJIEFF
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7722160
• 关键词: Alcohol Oxidoreductases; Biological Factors; California; Collection; Complex; Computer Retrieval of Information on Scientific Projects Database; Cysteine; Data; Data Collection; Drosophila melanogaster; Enzymes; Flavoproteins; Funding; Grant; Institution; Molecular; Molecular Chaperones; Myosin ATPase; NADPH Oxidoreductases NADH; Numbers; Oxidoreductase; Peptides; Process; Proteins; RNA; Recombinants; Research; Research Personnel; Resolution; Resources; Source; Sulfur; Time; United States National Institutes of Health; Universities; Yeasts; Zeolites; base; cytochrome c; desire; inhibitor/antagonist; mutant; nanobiotechnology; novel; protein structure; secretase; three dimensional structure

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. 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 ?-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.

这个子项目是许多利用 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。列出的机构为 研究中心，而研究中心不一定是研究者所在的机构。 加州州立大学和几个主要本科院校的研究涉及确定生物纳米技术、生物医学、环境和工业过程中重要的蛋白质、肽和酶的3D结构。SSRL对光束时间的要求集中在收集细菌细胞色素c？的高分辨率衍射数据，一种来自果蝇的新型肌球蛋白折叠伴侣，酵母羰基还原酶突变体，参与硫还原的单半胱氨酸黄素蛋白NAD（P）H氧化还原酶，一种来自海栖栖热加的新型RNA保护酶TM 0159，重组？与天然产物抑制剂复合的分泌酶、几种酶（复合物和突变体）和基于螺旋肽的生物沸石。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射线源来说太小或太敏感。虽然大多数蛋白质结构可以通过分子置换来确定，但至少有一种需要准确的MAD数据收集。