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缓激肽在水溶液中的构象多样性。

Conformational diversity of bradykinin in aqueous solution.

作者信息

Denys L, Bothner-By A A, Fisher G H, Ryan J W

出版信息

Biochemistry. 1982 Dec 7;21(25):6531-6. doi: 10.1021/bi00268a032.

DOI:10.1021/bi00268a032
PMID:7150573
Abstract

The 600-MHz proton nuclear magnetic resonance spectra of bradykinin, [2-dehydroproline]bradykinin, [7-dehydroproline]bradykinin, and [5-tyrosine]bradykinin in aqueous solution have been 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 proline-7 and phenylalanine-8, as well as a change in side-chain rotameric preference.

摘要

已记录了缓激肽、[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600兆赫质子核磁共振谱,并通过pH变化、自旋-自旋去耦和化学位移相关性对其进行了完全归属。对主链和侧链中自旋-自旋耦合常数的分析表明,缓激肽在许多构象异构体之间处于快速平衡状态,并且没有显示出任何持久的结构特征,如β转角或内部氢键。高浓度添加脂质或类脂质材料[如(三甲基硅基)丙酸钠]会导致光谱发生变化,表明与脯氨酸-7和苯丙氨酸-8存在特异性相互作用,以及侧链旋转异构体偏好发生变化。

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