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Infrared Dichroism of Isotope-edited alpha-Helices and beta-Sheets.

机译:同位素编辑的alpha-Helices和beta-Sheets的红外二向色性。

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摘要

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.
机译:酰胺红外谱带的同位素编辑不仅可以定位蛋白质中的二级结构元素,还可以生成构象信息,如果不进行同位素编辑,该信息不能从比对样品的线性二色性中获得。本文介绍了通过结合使用不同的酰胺基带和几个标记位置可以得出的关于膜中α螺旋取向分布的其他信息。而且,明确地考虑了过渡力矩的方位角取向与蛋白质结构之间的关系。首次对β-折叠片和β-桶的红外二色性进行了全面分析。对于这种分析必不可少的β-折叠中各个跃迁矩的方向是针对不同的酰胺基带得出的。

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