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首页> 外文期刊>Biochemistry >Backbone dynamics of azurin in solution: slow conformational change associated with deprotonation of histidine 35.
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Backbone dynamics of azurin in solution: slow conformational change associated with deprotonation of histidine 35.

机译：溶液中天青蛋白的骨干动力学：与组氨酸35去质子化有关的缓慢构象变化。

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摘要

15N relaxation measurements have been performed on the type Iota blue copper protein azurin from Pseudomonas aeruginosa. The relaxation times show that one loop (residues 103-108) and one turn (residues 74-77) display fast internal motions. The rest of the protein is rigid with an average order parameter S(2) of 0.85 +/- 0. 05. The copper binding site shows the same degree of rigidity even though is it composed of several loops and lies outside the beta-sheet sandwich. Substantial exchange broadening was found for a number of residues surrounding the side chain of His-35. The average exchange rate has been determined from NMR exchange spectroscopy experiments and is 45 +/- 6 s(-)(1) at 41 degrees C. The exchange broadening is caused by the protonation/deprotonation equilibrium of His-35. The NMR results indicate that the two structures of azurin observed by X-ray diffraction of crystals at pH 5.5 and 9.0 [Nar, H., Messerschmidt, A., Huber, R., Van de Kamp, M., Canters, G. W. (1991) J. Mol. Biol. 221, 765-772] are present in solution and that they interconvert slowly.
机译：对来自铜绿假单胞菌的Iota蓝色铜蛋白天青蛋白进行了15N弛豫测量。弛豫时间表明，一个循环（残基103-108）和一转（残基74-77）显示出快速的内部运动。其余的蛋白质是刚性的，平均阶数参数S（2）为0.85 +/-0。05.铜结合位点显示出相同程度的刚性，即使它由多个环组成并且位于beta折叠之外三明治。发现His-35侧链周围的许多残基有大量交换加宽。平均交换速率已通过NMR交换光谱实验确定，在41摄氏度下为45 +/- 6 s（-）（1）。交换增宽是由His-35的质子/去质子平衡引起的。 NMR结果表明，通过在pH 5.5和9.0的晶体X射线衍射观察到的天青蛋白的两个结构[Nar，H.，Messerschmidt，A.，Huber，R.，Van de Kamp，M.，Canters，GW（ 1991）J.Mol。生物学221，765-772]存在于溶液中，并且它们缓慢地相互转化。

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