CRYSTALLOGRAPHIC STUDIES OF LARGE MACROMOLECULAR ASSEMBLIES

大分子组装体的晶体学研究

• 批准号: 8169218
• 负责人: THOMAS Arthur STEITZ
• 金额: $ 4.88万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169218
• 关键词: Amino Acyl-tRNA Synthetases; Antibiotics; Binding; Complex; Computer Retrieval of Information on Scientific Projects Database; Cyclic AMP; DNA; DNA Primase; DNA-Directed RNA Polymerase; DnaB helicase; Escherichia coli; Funding; Grant; Institution; Ligands; Molecular Biology; Nucleic Acids; Proteins; Research; Research Personnel; Resources; Ribosomes; Source; Structure; United States National Institutes of Health; macromolecular assembly; novel; tau Proteins

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. Structural studies of proteins and nucleic acids and the complexes they make that are involved in executing Crick's Central Dogma of Molecular Biology are the subjects of our ongoing studies. The structures being pursued include complexes between the components of the bacterial replisome - DnaB helicase complexed with primase and DNA as well as complexes with a fragment of Tau; E. coli RNA polymerase complexed with DNA; CAP without ligands and CAP with cAMP bound to DNA with RNA polymerase; novel aminacyl-tRNA synthetases complexed with substrates; structures of the 70S ribosome complexed with substrates, factors, or antibiotics; complexes between the 50S ribosomal subunit and antibiotics; structural studies of the eukaryotic ribosomes.

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