One- and two- dimensional 15N/1H NMR of filamentous phage coat proteins in solution.
One- and two- dimensional 15N/1H NMR of filamentous phage coat proteins in solution.
复制标题
溶液中丝状噬菌体外壳蛋白的一维和二维 15N/1H NMR。
DOI：
10.1016/s0006-291x(85)80193-5
复制
发表时间：
1985
影响因子：
3.1
通讯作者：
Opella,SJ
中科院分区：
文献类型：
--
作者：
Bogusky,MJ;Tsang,P;Opella,SJ
通过结合使用同位素富集的蛋白质和脉冲序列，可以有效地进行溶液中蛋白质的高分辨率15n NMR研究，脉冲序列产生质子的极化转移，并产生二维异核化学位移相关光谱。丝状噬菌体fd和pf1溶解在洗涤剂胶束中的外壳蛋白给出了几乎所有蛋白质中氮位点的一维和二维核磁共振光谱。通过比较pH=4.0时D2O和H2O溶液中蛋白质的光谱，可以得到质子缓慢交换的酰胺位点的共振，作为所有酰胺位点共振的一个子集。
High resolution15N NMR studies of proteins in solution can be performed efficiently by combining the use of isotopically enriched proteins and pulse sequences that generate polarization transfer from protons and result in two-dimensional heteronuclear chemical shift correlation spectra. The coat proteins of the filamentous bacteriophages fd and Pf 1 solubilized in detergent micelles give one- and two- dimensional NMR spectra with resolved resonances for nearly all of the nitrogen sites in the proteins. The resonances from the amide sites with slowly exchanging protons can be obtained as a subset of the resonances of all amide sites by comparing the spectra of proteins in D2O and H2O solutions at pH=4.0.