Assignment of proximal histidine proton NMR peaks in myoglobin and hemoglobin.
Assignment of proximal histidine proton NMR peaks in myoglobin and hemoglobin.
复制标题
肌红蛋白和血红蛋白中近端组氨酸质子 NMR 峰的分配。
DOI：
10.1016/s0006-291x(77)80170-8
复制
发表时间：
1977
影响因子：
3.1
通讯作者：
H. Goff
中科院分区：
文献类型：
--
作者：
G. L. La Mar;D. Budd;H. Goff
脱氧肌红蛋白和血红蛋白模型化合物的质子核磁共振谱归属为咪唑的轴向共振。这些信息直接导致了抹香鲸脱氧肌红蛋白中所有三个近端组氨酰咪唑质子共振的归属，以及脱氧血红蛋白A中α和β链的两个不等价近端组氨咪唑NH信号。NH峰有望成为血红蛋白T⇌R转变的有价值的探针。
The proton nmr spectra of model compounds of deoxy myoglobin and hemoglobin have yielded the assignment of the axial imidazole resonances. The information leads directly to an assignment of all three proximal histidyl imidazole proton resonances in sperm whale deoxy myoglobin, and the two non-equivalent proximal histidyl imidazole NH signals of the α and β chains in deoxy hemoglobin A. The NH peaks are expected to serve as valuable probes for the T ⇌ R transition in hemoglobins.