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The transmembrane domains of the nicotinic acetylcholine receptor contain alpha-helical and beta structures.

机译:烟碱乙酰胆碱受体的跨膜结构域包含α-螺旋和β结构。

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摘要

The transmembrane domain of the nicotinic acetylcholine receptor (nAChR) from Torpedo californica electric tissue contains both alpha-helical and beta structures. The secondary structure was investigated by Fourier transform infrared (FTIR) spectroscopy after the extramembrane moieties of the protein from the extracellular and intracellular sides of the membrane were removed by proteolysis using proteinase K. The secondary structure composition of this membrane structure was: alpha-helical 50%, beta structure and turns 40%, random 10%. The alpha-helices are shown to be oriented with respect to the membrane plane in a way allowing them to span the membrane, while no unidirectional structure for the beta structures was observed. These findings contradict previous secondary structure models based on hydropathy plots alone.
机译:来自加利福尼亚鱼雷电组织的烟碱乙酰胆碱受体(nAChR)的跨膜结构域包含α-螺旋结构和β结构。使用蛋白酶K通过蛋白水解作用从膜的细胞外和细胞内侧面除去蛋白质的膜外部分后,通过傅里叶变换红外(FTIR)光谱研究了二级结构。该膜结构的二级结构组成为:α-螺旋50%,β结构和旋转40%,随机10%。示出了α-螺旋相对于膜平面以允许它们跨过膜的方式取向,而没有观察到β结构的单向结构。这些发现与仅基于亲水性图的先前二级结构模型相矛盾。

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