首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Deuteration can affect the conformational behaviour of amphiphilic alpha-helical structures.
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Deuteration can affect the conformational behaviour of amphiphilic alpha-helical structures.

机译:氘化可影响两亲性α-螺旋结构的构象行为。

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摘要

The replacement of hydrogen with deuterium is frequently used in conjunction with neutron diffraction to investigate peptide-membrane interaction. This isotopic substitution in an amino acid residue radically changes the neutron scatter pattern of the peptide, thereby allowing its localisation within the bilayer with the aid of derived Fourier maps. Nonetheless, this technique relies on the generally held assumption that normal and isotopically enriched protein species do not differ significantly in structure or biological activity. Recently, this assumption has been questioned and here, diffraction data from studies on a membrane interactive peptide clearly challenge the reliability of this assumption.
机译:用氘置换氢经常与中子衍射结合使用,以研究肽-膜相互作用。氨基酸残基中的这种同位素取代会从根本上改变肽的中子散射模式,从而借助衍生的傅立叶图谱将其定位在双层中。但是,该技术依赖于通常认为的正常和同位素富集的蛋白质种类在结构或生物学活性上没有显着差异的假设。最近,对该假设提出了质疑,在这里,来自膜相互作用肽研究的衍射数据明显挑战了该假设的可靠性。

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