Infrared dichroism of isotope-edited α-helices and β-sheets
Infrared dichroism of isotope-edited α-helices and β-sheets
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DOI：
10.1016/j.jmb.2004.02.061
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发表时间：
2004-04-23
影响因子：
5.6
通讯作者：
Marsh, D
中科院分区：
文献类型：
--
作者：
Marsh, D
酰胺红外谱带的同位素编辑不仅定位了蛋白质中的二级结构元素，而且还产生了在没有同位素编辑的情况下无法从排列的样品的线性二色性中获得的构象信息。通过结合使用不同的酰胺带和标记的几个位置，可以获得关于膜中α-螺旋的取向分布的附加信息。此外，还讨论了跃迁力矩的方位向与蛋白质结构之间的关系。本文首次对贝塔薄片和贝塔桶的红外二色性进行了全面的分析。对于不同的酰胺带，推导出了该分析所必需的β-折叠中各个转变力矩的方向。(C)2004爱思唯尔有限公司。保留所有权利。
Isotope editing of amide infrared bands not only localises secondary structural elements within the protein but also yields conformational information that is not available from the linear dichroism of aligned samples without isotope editing. The additional information that can be derived on the orientational distribution of alpha-helices in membranes by the combined use of different amide bands and several positions of labelling is presented here. Also, the relationship between the azimuthal orientation of the transition moment and the protein structure is treated explicitly. A comprehensive analysis of the infrared dichroism for beta-sheets and beta-barrels is given here, for the first time. The orientation of the individual transition moments in a beta-sheet that is essential for this analysis is derived for the different amide bands. (C) 2004 Elsevier Ltd. All rights reserved.