Ottaviani M F, Huinink H, Sanders J C, Hemminga M A
Department of Chemistry, University of Florence, Italy.
Biochim Biophys Acta. 1993 Oct 10;1152(1):171-6. doi: 10.1016/0005-2736(93)90244-t.
The coat protein of the bacteriophage M13 in the alpha-helical state is reconstituted in macroscopically oriented systems of dioleoylphosphatidylcholine that are prepared by squeezing the reconstituted material between glass plates. The coat protein dramatically influences the macroscopic orientation of the multibilayers, as is investigated by polarizing microscopy and EPR spectroscopy of the cholestane spin label embedded in the bilayers. It is found that with increasing amounts of protein the spontaneous macroscopic orientation of the reconstituted system decreases. This effect is proposed to be due to an increase of the apparent viscosity of the lipid-protein systems with increasing amounts of protein. This is assumed to arise from a sticky effect of the C- and N-terminal protein parts that extend into the aqueous phase between the bilayers.
处于α-螺旋状态的噬菌体M13的外壳蛋白在由二油酰磷脂酰胆碱构成的宏观取向系统中重构，该系统通过将重构材料挤压在玻璃板之间制备。外壳蛋白极大地影响多层膜的宏观取向，这通过偏振显微镜和嵌入双层中的胆甾烷自旋标记的电子顺磁共振光谱进行研究。发现随着蛋白质数量的增加，重构系统的自发宏观取向降低。这种效应被认为是由于脂质-蛋白质系统的表观粘度随着蛋白质数量的增加而增加。这被假定源于延伸到双层之间水相中的C端和N端蛋白质部分的粘性效应。
