A binding site peptide fragment of the nicotinic acetylcholine receptor. Sequence-specific assignment of 1H-NMR resonances in the dodecamer alpha 185-196.
A binding site peptide fragment of the nicotinic acetylcholine receptor. Sequence-specific assignment of 1H-NMR resonances in the dodecamer alpha 185-196.
复制标题
烟碱乙酰胆碱受体的结合位点肽片段。
DOI：
10.1016/0006-2952(90)90179-o
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发表时间：
1990
影响因子：
5.8
通讯作者：
Hawrot,E
中科院分区：
文献类型：
--
作者：
Song,GQ;Armitage,IM;Hawrot,E
通过分析COSY光谱沿着自旋去耦和确证性NOE差异实验，完成α 185-肽的总序列特异性1H归属。利用具有选择性氨基酸取代的额外肽成功地解决了分配中的一些模糊性。几个C α H共振的化学位移，沿着Thr-191处缓慢交换酰胺的证据表明，α 185-肽可能含有一定量的非无规卷曲结构。任何这种有序结构在与α-银环蛇毒素结合的机制中的作用仍有待确定。肽1H共振的归属将有助于分析和鉴定α-银环蛇毒素和α 185-肽之间形成复合物时观察到的化学位移扰动[7]。
The total sequence-specific 1H assignment for the alpha 185-peptide was accomplished by analysis of COSY spectra along with spin-decoupling and confirmatory NOE difference experiments. Some ambiguities in the assignments were successfully addressed utilizing additional peptides with selective amino acid substitutions. The chemical shifts of several of the C alpha H resonances, along with evidence for a slowly exchanging amide at Thr-191 suggest that the alpha 185-peptide may contain a certain amount of non-random coil structure. The role of any such ordered structure in the mechanism of binding to alpha-bungarotoxin remains to be determined. The assignment of the peptide 1H resonances will facilitate the analysis and identification of chemical shift perturbations observed upon formation of the complex between alpha-bungarotoxin and the alpha 185-peptide [7].