NEW SOFTWARE FOR OPERATION OF PULSE PROGRAMMER TO IMPLEMENT HYSCORE

用于操作 Pulse 编程器以实施 HYSCORE 的新软件

• 批准号: 6121154
• 负责人: WENYU WANG
• 金额: $ 1.17万
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-05-05 至 2000-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6121154
• 关键词: bioengineering /biomedical engineering; biological products; biomaterials; biomedical equipment development; biomedical resource; technology /technique

ESEEM studies at 7.8, 9.5, and 10.8 GHz were initiated in order to investigate the ligand structure and charge symmetry of the high and low pH forms of the protein. ESEEM spectra suggest that there are two imidazoles coordinated to copper, with coupling to two nitrogens (a measure of spin delocalization for the Cu d9 configuration) differing. The ESEEM spectra of high and low pH forms of the protein are qualitatively identical. However, the change of width in combination lines of the spectrum indicate reorganization of relative geometry of the two imidazoles at elevated pH. There is no indication of a new ligands at high pH. Furthermore, the quadrupole parameters of the remote imidazole nitrogen atoms are unchanged. The only apparent difference between the two proteins is the magnitude of the nuclear hyperfine coupling, which seems to be less in the high pH form of the protein. A paper on the Rhus stellacyanin has been accepted for

启动 7.8、9.5 和 10.8 GHz 的 ESEEM 研究是为了 研究高和低配体的配体结构和电荷对称性 蛋白质的低pH形式。 ESEEM 谱表明有两个 咪唑与铜配位，与两个氮（一个 Cu d9 配置的自旋离域测量）不同。 高和低 pH 形式蛋白质的 ESEEM 光谱为 质量相同。 然而，组合宽度的变化 谱线表明相对几何形状的重组 两种咪唑在升高的pH值下发生反应。 没有迹象表明有新的 高pH值下的配体。 此外，四极杆参数 远程咪唑氮原子未改变。 唯一明显的 两种蛋白质之间的差异在于核的大小 超精细耦合，在高 pH 形式中似乎较少 蛋白质。 一篇关于漆树花青素的论文已被接受