蛋白质三维图像中β-链扭曲的分析。

Tunazzina Islam, Michael Poteat, Jing He
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引用次数: 0

摘要

电子冷冻显微镜(Cryo-EM)技术产生分子的三维(3D)图像的密度图。从中等分辨率的三维图像中推导蛋白质的原子结构是一项具有挑战性的工作。人们对β-链的扭曲进行了广泛的研究,但从β-片的三维图像中直接获得的已知信息很少。我们描述了一种方法来表征β-链的扭曲从三维图像的蛋白质。对11张β薄片图像的分析表明,平均最小扭转(AMT)角对于近组β痕迹比远组β痕迹更大。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Analysis of β-strand Twist from the 3-dimensional Image of a Protein.

Electron cryo-microscopy (Cryo-EM) technique produces density maps that are 3-dimensional (3D) images of molecules. It is challenging to derive atomic structures of proteins from 3D images of medium resolutions. Twist of a β-strand has been studied extensively while little of the known information has been directly obtained from the 3D image of a β-sheet. We describe a method to characterize the twist of β-strands from the 3D image of a protein. An analysis of 11 β-sheet images shows that the Averaged Minimum Twist (AMT) angle is larger for a close set than for a far set of β-traces.

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