进化对金枪鱼肌红蛋白结构的影响。

The effect of evolution on the structure of tuna myoglobin.

作者信息

Bismuto E, Savy F, Irace G, Colonna G

出版信息

Boll Soc Ital Biol Sper. 1983 Dec 30;59(12):1773-9.

Abstract

The circular dichroic activity of tuna myoglobin in the far ultraviolet has been found to be lower than that of mammalian myoglobin, thus indicating a lower content of alpha-helix. Fluorescence and absorption studies have indicated that the structure of the N-terminal region of the molecule is essentially the same in all the examined apomyoglobins, whereas differences have been observed in the heme microenvironment. The prediction of secondary structure has revealed that the alpha-helical segments of tuna myoglobin, especially those involved in the formation of the heme pocket, are shorter than those of sperm whale myoglobin.

摘要

已发现金枪鱼肌红蛋白在远紫外区的圆二色活性低于哺乳动物肌红蛋白，因此表明α-螺旋含量较低。荧光和吸收研究表明，在所有检测的脱辅基肌红蛋白中，分子N端区域的结构基本相同，而在血红素微环境中观察到了差异。二级结构预测显示，金枪鱼肌红蛋白的α-螺旋片段，尤其是那些参与血红素口袋形成的片段，比抹香鲸肌红蛋白的短。