STRUCTURAL STUDIES OF HYPERTHERMOPHILIC PROTEINS

超嗜热蛋白质的结构研究

• 批准号: 7370349
• 负责人: SUNG-HOU KIM
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370349
• 关键词: STRUCTURAL; STUDIES; HYPERTHERMOPHILIC; 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. We are investigating the proteins from several hyperthermophiles. The structural assay will provide basis for understanding of the thermal stability of proteins from hyperthermophilic organisms, and functions of "hypothetical" proteins of unknown function. We currently have four hyperthermophilic proteins expressed and crystallized in both wild-type and Se-Met derivative forms. This group includes two annotated protein -- NusG and FAD synthetase, and two hypothetical proteins. The crystallographic investigation of the above crystals requires high intensity X-ray sources at adjustable multiple wavelengths for MAD phasing.

该子项目是利用 NIH/NCRR 资助的中心拨款提供的资源的众多研究子项目之一。子项目和研究者 (PI) 可能已从另一个 NIH 来源获得主要资金，因此可以在其他 CRISP 条目中得到体现。列出的机构是中心的机构，不一定是研究者的机构。我们正在研究来自几种超级嗜热菌的蛋白质。结构测定将为了解来自超嗜热生物体的蛋白质的热稳定性以及功能未知的“假设”蛋白质的功能提供基础。我们目前有四种超嗜热蛋白以野生型和 Se-Met 衍生物形式表达和结晶。该组包括两种注释蛋白——NusG 和 FAD 合成酶，以及两种假设蛋白。上述晶体的晶体学研究需要可调节多个波长的高强度 X 射线源以进行 MAD 定相。