NIH ADMINISTRATIVE SUPPLEMENT AUTOMATED PEPTIDE SYNTHESIZER ZHUANG

NIH 行政补充自动肽合成仪庄

• 批准号: 10387411
• 负责人: Zhihao Zhuang
• 金额: $ 6.97万
• 依托单位: UNIVERSITY OF DELAWARE
• 依托单位国家: 美国
• 财政年份: 2019
• 资助国家: 美国
• 起止时间: 2019-04-01 至 2023-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/10387411
• 关键词: ATP phosphohydrolase; Administrative Supplement; Affinity; Binding; Binding Proteins; Biochemical; Bioinformatics; Biological Assay; Biological Process; Biotin; Bypass; Cell physiology; Cells; Chemicals; Complex; Crosslinker; Cryoelectron Microscopy; Cyclooctenes; DNA; DNA Binding; DNA Damage; DNA biosynthesis; DNA replication fork; Data; Development; Ensure; Eukaryota; Event; Generations; Goals; Homologous Gene; Human; Individual; Investigation; Label; Length; Lesion; Ligation; Link; Lysine; Mass Spectrum Analysis; Mediating; Methods; Modeling; Modification; Orthologous Gene; Parents; Pathway interactions; Peptide Synthesis; Peptides; Phase; Polyubiquitin; Polyubiquitination; Proteins; Reader; Research; Resistance; Role; Signal Transduction; Solid; Streptavidin; Structure; System; Technology; Testing; Therapeutic Intervention; UV induced; Ubiquitin; Ubiquitination; United States National Institutes of Health; Yeasts; crosslink; multicatalytic endopeptidase complex; mutant; novel; novel strategies; novel therapeutic intervention; protein degradation; reconstitution; recruit; response; success; thioether; unnatural amino acids

ABSTRACT This supplement is requested to support R01 GM129468: Decoding the non-canonical polyubiquitin chains using chemical approaches. The goal of the parent proposal is to develop new approaches for protein polyubiquitination and subsequent identification and characterization of readers of the noncanonical ubiquitin chains in DNA damage tolerance. The success of this proposal critically depends on the ability to generate modified ubiquitin species that contain reactive linker molecules or unnatural amino acids. Using automated solid-phase peptide synthesis (SPPS) to generate the critical ubiquitin species in sufficiently large quantity will ensure the success of proposed research.

摘要 本补充要求支持R01 GM129468：解码非规范 使用化学方法的聚泛蛋白链。家长提案的目标是发展 蛋白质多聚泛素化及随后的鉴定和表征的新方法 在DNA损伤耐受中的非典型泛素链的读者。的成功 该提议关键取决于产生修饰的泛素种类的能力，所述修饰的泛素种类包含 反应性接头分子或非天然氨基酸。使用自动化固相肽 合成（SPPS）以产生足够大量的关键泛素物质将确保 所提出的研究的成功。

项目成果

Chemical methods for protein site-specific ubiquitination.

• DOI: 10.1039/d0cb00215a
• 发表时间: 2021-04-01
• 期刊: RSC chemical biology
• 影响因子: 4.1
• 作者: Gui W;Davidson GA;Zhuang Z
• 通讯作者: Zhuang Z