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Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy

机译:髓鞘碱性蛋白质同种型与FTIR光谱研究的脂质双层的相互作用

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ondary structure of the naturally occurring isoforms of myelin basic protein (MBP1-8) from human myelin was studied by Fourier transform infrared spectroscopy under a variety of experimental conditions. In aqueous solution each isoform was found to be unstructured. In the presence of negatively charged liquid bilayers MBP1-4 were shown to exhibit an amide I band maximum indicative of the adoption of $alpha@-helical secondary structures. A detailed analysis revealed that significant proportions of $beta@-sheet secondary structure were also present. MBP5 and MBP8, which have significantly less cationic charge than MBP1-4, exhibited an amide I maximum identical to that seen in solution, suggesting that no interaction with the bilayer occurred. Analysis of the lipid CH$-2$/ and C $EQ O stretching vibrations also pointed towards significant interaction of MBP1-4 with the bilayer. The changes in intensity and frequency of these bands which typically accompany the phase transition in the pure bilayer were abolished by addition of the proteins. No such effect was seen for MBP5 and 8, the normal lipid phase transition being apparent. The implications of these results in the aetiology of multiple sclerosis is discussed.
机译:在各种实验条件下,通过傅里叶变换红外光谱研究了来自人髓鞘的髓鞘碱性蛋白质(MBP1-8)的天然存在的同种型的欧洲族结构。在水溶液中,发现每种同种型都是非结构化的。在存在带负电荷的液体双层中,显示MBP1-4表现出酰胺I频段最大值,其采用$ alpha @-helical二级结构。详细分析显示,还存在大量比例的$ BETA @ -Sheet二级结构。 MBP5和MBP8具有比MBP1-4显着更少阳离子电荷的MBP8,展示了酰胺I最大与溶液中所见的酰胺相同的酰胺,这表明没有发生与双层的相互作用。脂质CH $ -2 $ /和C $ eq o拉伸振动的分析也指出了MBP1-4与双层的显着相互作用。通过添加蛋白质,废除了通常伴随纯双层中相转变的这些带的强度和频率的变化。对于MBP5和8,没有看到这种效果,正常的脂质相转变是显而易见的。讨论了这些结果在多发性硬化症的病症中的影响。

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