Song G Q, Armitage I M, Hawrot E
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510.
Biochem Pharmacol. 1990 Jul 1;40(1):63-5. doi: 10.1016/0006-2952(90)90179-o.
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].
通过分析COSY谱以及自旋去耦和验证性NOE差异实验，完成了α185肽的全序列特异性1H归属。利用具有选择性氨基酸取代的其他肽成功解决了归属中的一些模糊性问题。几个CαH共振的化学位移，以及Thr-191处酰胺缓慢交换的证据表明，α185肽可能包含一定量的非随机卷曲结构。任何这种有序结构在与α-银环蛇毒素结合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在α-银环蛇毒素与α185肽形成复合物时观察到的化学位移扰动[7]。
