通过中子衍射对复性细菌视紫红质结构中两个胰凝乳蛋白酶片段进行定位
Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction.
作者信息
Trewhella J, Popot J L, Zaccaï G, Engelman D M
出版信息
EMBO J. 1986 Nov;5(11):3045-9. doi: 10.1002/j.1460-2075.1986.tb04604.x.
Abstract
The structure of crystalline purple membrane reconstituted from purified bacteriorhodopsin (BR) chymotryptic fragments has been studied by neutron diffraction. In one of the samples studied, the fragment C-2, encompassing the first two predicted transmembrane segments, was prepared from deuterated purple membrane. The diffraction changes when the natural C-2 fragment is substituted by a deuterated one are analysed in terms of a seven-helix model for BR. The assignment of the labelled fragment to one end of the molecule placed new constraints on folding models for the protein.
摘要
通过中子衍射研究了由纯化的细菌视紫红质（BR）胰凝乳蛋白酶片段重构的结晶紫膜的结构。在研究的一个样品中，包含前两个预测跨膜片段的片段C-2是由氘代紫膜制备的。根据BR的七螺旋模型分析了天然C-2片段被氘代片段取代时的衍射变化。将标记片段定位到分子的一端，这对蛋白质的折叠模型提出了新的限制。
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