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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles.
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Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles.

机译:两跨膜螺旋肽与脂质双层和十二烷基硫酸盐微团的相互作用。

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摘要

To probe structural changes that occur when a membrane protein is transferred from lipid bilayers to SDS micelles, a fragment of bacteriorhodopsin containing transmembrane helical segments A and B was studied by fluorescence spectroscopy, molecular dynamics (MD) simulation, and stopped flow kinetics. In lipid bilayers, Forster resonance energy transfer (FRET) was observed between tyrosine 57 on helix B and tryptophans 10 and 12 on helix A. FRET efficiency decreased substantially when the peptide was transferred to SDS. MD simulation showed no evidence for significant disruption of helix-helix interactions in SDS micelles. However, a cluster of water molecules was observed to form a hydrogen-bonded network with the phenolic hydroxyl group of tyrosine 57, which probably causes the disappearance of tyrosine-to-tryptophan FRET in SDS. The tryptophan quantum yield decreased in SDS, and the change occurred at nearly the same rate as membrane solubilization. The results provide a clear example of the importance of corroborating distance changes inferred from FRET by using complementary methods.
机译:为了探测当膜蛋白从脂质双层转移到SDS胶束时发生的结构变化,通过荧光光谱,分子动力学(MD)模拟和停止流动动力学研究了含有视紫红质的跨膜螺旋段A和B的细菌视紫红质的片段。在脂质双层中,在螺旋B上的酪氨酸57和螺旋A上的色氨酸10和12之间观察到Forster共振能量转移(FRET)。当肽转移到SDS时,FRET效率大大降低。 MD模拟显示没有证据表明SDS胶束中的螺旋-螺旋相互作用显着破坏。但是,观察到一团水分子与酪氨酸57的酚羟基形成氢键网络,这可能导致SDS中酪氨酸到色氨酸FRET的消失。 SDS中的色氨酸量子产率下降,并且该变化的发生速率几乎与膜溶解的速率相同。结果提供了一个清晰的例子,证明了通过使用互补方法来验证FRET推断出的距离变化的重要性。

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