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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Wide-angle X-ray scattering as a probe for insulin denaturation
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Wide-angle X-ray scattering as a probe for insulin denaturation

机译：广角X射线散射作为胰岛素变性的探针

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摘要

Wide-angle X-ray scattering (WAXS) from lyophilized protein is characterized by the presence of two relatively broad scattering peaks that are linked to protein structure. This work is concerned with the possibility of utilizing these peaks in the probing of the unfolding and breakdown of insulin. Native insulin is subject to thermal denaturation in the presence and in the absence of thiol catalysts. Denatured products are acid-trapped, lyophilized and monitored using WAXS in addition to Fourier transform infrared spectroscopy (FTIR), gel filtration chromatography and Transmission Electron Microscopy (TEM) as supportive techniques. Results show that the WAXS peak at a d-spacing about 10 A is sensitive towards the a-helix content of insulin. A reduction in the intensity of such peak is proven to be directly linked to the reduction of native insulin having normal a-helix content. The supportive techniques confirmed the decrease in the a-helix content of insulin which accompanied the different denaturation treatments.
机译：冻干蛋白质的广角X射线散射（WAXS）的特征是存在两个与蛋白质结构相关的相对较宽的散射峰。这项工作与在胰岛素的展开和分解的探测中利用这些峰的可能性有关。在存在和不存在硫醇催化剂的情况下，天然胰岛素都会发生热变性。除傅立叶变换红外光谱（FTIR），凝胶过滤色谱和透射电子显微镜（TEM）之外，还使用WAXS对变性的产物进行酸捕获，冻干和监测，以作为辅助技术。结果表明，在大约10 A的d间隔处的WAXS峰对胰岛素的a螺旋含量敏感。证实该峰强度的降低与具有正常α-螺旋含量的天然胰岛素的降低直接相关。支持技术证实了伴随不同变性处理的胰岛素α-螺旋含量的降低。

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