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大肠杆菌核糖体蛋白S4的构象预测与圆二色性研究

Conformational prediction and circular dichroism studies on ribosomal protein S4 from Escherichia coli.

作者信息

Allen S H, Wong K P

出版信息

Biophys J. 1978 Sep;23(3):359-73. doi: 10.1016/S0006-3495(78)85455-1.

Abstract

The conformation of ribosomal protein S4 from Escherichia coli has been studied by circular dichroism (CD) and shown to possess unique conformation free in solution. The near ultraviolet spectrum suggests the existence of unique tertiary structural environment for the aromatic amino acid residues. The far ultraviolet spectrum gives an estimation of its secondary structure which is 32% alpha-helix and 14% beta-structure in reconstitution buffer at 25 degrees C. The conformation of S4 has been predicted from its sequence, and two models are presented here. An attempt is made to correlate these two molecular models with the available physicochemical data concerning the shape, conformation, and possible RNA binding site of protein S4.

摘要

通过圆二色性(CD)研究了来自大肠杆菌的核糖体蛋白S4的构象,结果表明其在溶液中具有独特的构象。近紫外光谱表明芳香族氨基酸残基存在独特的三级结构环境。远紫外光谱给出了其二级结构的估计值,在25℃的重构缓冲液中,其二级结构为32%的α-螺旋和14%的β-结构。已根据S4的序列预测了其构象,本文给出了两种模型。试图将这两种分子模型与有关蛋白S4的形状、构象和可能的RNA结合位点的现有物理化学数据相关联。

相似文献

本文引用的文献

1
CIRCULAR DICHROISM OF POLY-L-TYROSINE.聚-L-酪氨酸的圆二色性
Biochemistry. 1964 Nov;3:1675-8. doi: 10.1021/bi00899a012.
3
A computerized calibration of the circular dichrometer.圆二色仪的计算机校准
Biochemistry. 1969 May;8(5):1947-51. doi: 10.1021/bi00833a026.

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