Dmitriev Oleg Y, Abildgaard Frits, Markley John L, Fillingame Robert H
J Biomol NMR. 2004 Jul;29(3):439-40. doi: 10.1023/B:JNMR.0000032519.14221.20.
The structure of the 30 KDa subunit a of the membrane component (F(0)) of E. coli ATP synthase is investigated in a mixture of chloroform, methanol and water, a solvent previously used for solving the structure of another integral membrane protein, subunit c. Near complete backbone chemical shift assignments were made from a set of TROSY experiments including HNCO, HNCA, HN(CA)CB, HN(CO)CACB and 4D HNCOCA and HNCACO. Secondary structure of subunit a was predicted from the backbone chemical shifts using TALOS program. The protein was found to consist of multiple elongated alpha-helical segments. This finding is generally consistent with previous predictions of multiple transmembrane alpha-helices in this polytopic protein.
在氯仿、甲醇和水的混合物中研究了大肠杆菌ATP合酶膜组分（F(0)）30 kDa亚基a的结构，该溶剂曾用于解析另一种整合膜蛋白亚基c的结构。通过一组TROSY实验（包括HNCO、HNCA、HN(CA)CB、HN(CO)CACB以及4D HNCOCA和HNCACO）完成了近乎完整的主链化学位移归属。使用TALOS程序根据主链化学位移预测了亚基a的二级结构。发现该蛋白质由多个伸长的α螺旋片段组成。这一发现与此前对该多结构域蛋白中多个跨膜α螺旋的预测总体一致。
