NEW SOFTWARE FOR OPERATION OF PULSE PROGRAMMER TO IMPLEMENT HYSCORE

开始在7.8、9.5和10.8 GHz进行ESEEM研究，以便 研究配体结构和电荷对称性的高， 低pH值的蛋白质。 ESEEM光谱表明，有两个 与铜配位的咪唑，与两个氮偶联（a Cu d9构型的自旋离域的测量）不同。 蛋白质的高pH和低pH形式的ESEEM光谱是 质量相同。 然而，组合中宽度的变化 谱线表明相对几何结构的重组， 两个咪唑在升高的pH值。没有迹象表明， 配体在高pH值。此外，四极参数的 远程咪唑氮原子不变。 唯一明显的 这两种蛋白质之间的差异是核的大小， 超精细偶联，在高pH形式中似乎较少 蛋白 一份关于漆树花青苷的论文已经被接受，

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