α-角蛋白中的中间丝。
Intermediate filaments in alpha-keratins.
作者信息
Fraser R D, MacRae T P, Parry D A, Suzuki E
出版信息
Proc Natl Acad Sci U S A. 1986 Mar;83(5):1179-83. doi: 10.1073/pnas.83.5.1179.
Abstract
Previous x-ray diffraction studies on the alpha-keratins of hair and wool have revealed that the intermediate filaments (IF) have a helical structure rendered imperfect by a precisely defined dislocation. It has also been possible to deduce a surface lattice for the IF and to determine the number of IF molecules associated with each lattice point. In this work this information is combined with data on the ionic interactions between the coiled-coil rope segments of the IF molecules to provide a plausible model for the pattern of interactions that stabilize the framework of the IF in the "hard" alpha-keratins. Similar interaction studies of the proteins from the IF in the so-called "soft" alpha-keratin from the stratum corneum layer of the skin suggest that they are likely to have an essentially similar pattern.
摘要
先前对毛发和羊毛的α-角蛋白进行的X射线衍射研究表明，中间丝（IF）具有一种螺旋结构，这种结构因精确确定的位错而变得不完美。人们还能够推导出中间丝的表面晶格，并确定与每个晶格点相关的中间丝分子数量。在这项工作中，这些信息与中间丝分子的卷曲螺旋绳段之间的离子相互作用数据相结合，以提供一个合理的相互作用模式模型，该模型可稳定“硬”α-角蛋白中中间丝的框架。对来自皮肤角质层中所谓“软”α-角蛋白的中间丝蛋白进行的类似相互作用研究表明，它们可能具有基本相似的模式。
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本文引用的文献
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