STRUCTURAL STUDIES OF HMG BOX PROTEIN NHP6A

以下两个项目是结构研究的一部分 大肠杆菌F0F1三磷酸腺苷合成酶在氯仿/甲醇/水中的c亚基 在我们实验室进行的溶剂。1.体内的c亚基形成a 由9-12个蛋白质分子组成的规则复合体。我们计划尝试引出 通过改变其组成在有机溶剂中形成络合物。这个 蛋白质的聚集状态将通过测量T1和 T2在反转恢复实验中。2.与本地人进行实验 酶显示我们实验室产生的其中一个c亚基突变体 可以特别地结合锂离子，这是一种最不寻常的性质，因为 野生型酶对H有绝对的特异性。我们会 研究纯化的突变蛋白是否与有机锂结合 溶剂型。目前正在进行的第一步是观察一维差异 在不同条件下采集的光谱qLi。因为大多数人 已经有野生型蛋白质、残留物的作业 参与与锂离子相互作用的元素可以通过 DQF-COSY实验。这个计划可能需要3-4个月的时间， 要求在DMX-600或DMX-500光谱仪上使用5 mm 1H探头。

The following two projects are a part of structural studies of subunit c of E. coli F0F1 ATP synthase in chloroform/methanol/water solvent conducted in our lab. 1. The c subunit in vivo forms a regular complex of 9-12 protein molecules. We plan to try to elicit complex formation in organic solvent by varying its composition. The aggregation state of the protein will be monitored by measuring t1 and t2 in inversion-recovery experiments. 2. Experiments with the native enzyme indicate that one of the c subunit mutants generated in our lab may specifically bind Li+ ions, a most unusual property, since the wild type enzyme displays absolute specificity for H+. We will investigate whether the purified mutant protein binds Li+ in organic solvent. The first step, now underway, is to look at 1D difference spectra collected under various conditions qLi+. Since most of the assignments are already available for wild type protein, residues involved in the interaction with Li+ ions could be identified by DQF-COSY experiments. This program will probably take 3-4 months and requires the use of 5 mm 1H-probe on DMX-600 or DMX-500 spectrometer.