CONFORMATIONAL DIVERSITY OF BRADYKININ IN AQUEOUS-SOLUTION
CONFORMATIONAL DIVERSITY OF BRADYKININ IN AQUEOUS-SOLUTION
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DOI：
10.1021/bi00268a032
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发表时间：
1982-01-01
期刊：
影响因子：
2.9
通讯作者：
RYAN, JW
中科院分区：
文献类型：
--
作者：
DENYS, L;BOTHNERBY, AA;RYAN, JW
记录了缓激肽、[2-脱氢脯氨酸]缓激肽、[7-脱氢脯氨酸]缓激肽和[5-酪氨酸]缓激肽在水溶液中的600 MHz PMR谱，并通过pH变化、自旋-自旋去耦和化学位移关联对谱进行了完全归属。主链和侧链中的自旋-自旋耦合常数的分析表明缓激肽在许多构象异构体中处于快速平衡，并且不显示任何持久的结构特征，例如β。转角或内部氢键。添加高浓度的脂质或脂质样物质[如（三甲基甲硅烷基）丙酸钠]会导致光谱发生变化，表明与Pro-7和Phe-8的特异性相互作用，以及侧链旋转异构体偏好的变化。
The 600 MHz PMR spectra of bradykinin, [2-dehydroproline]bradykinin, [7-dehydroproline]bradykinin, and [5-tyrosine]bradykinin in aqueous solution were recorded and completely assigned by means of pH variation, spin-spin decoupling and chemical shift correlations. Analysis of the spin-spin coupling constants in the main chain and in the side chains suggests that bradykinin is in rapid equilibrium among many conformers and does not show any persistent structural features such as .beta. turns or internal hydrogen bonds. Addition of lipids or lipid-like materials [such as sodium (trimethylsilyl)propionate] in high concentration causes changes in the spectra, indicating specific interactions with Pro-7 and Phe-8, and a change in side-chain rotameric preference.