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首页> 外文期刊>International Journal of Radiation Biology: Covering the Physical, Chemical, Biological, and Medical Effects of Ionizing and Non-ionizing Radiations >Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry.
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Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry.

机译：蛋白质表面的羟自由基探针使用同步加速器X射线辐射分解和质谱分析。

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摘要

A new approach is reported that combines synchrotron radiolysis and mass spectrometry to probe the structure of proteins. Hydroxyl radicals produced upon the radiolysis of protein solutions using synchrotron light modify amino acid side-chains on millisecond timescales. This results in the formation of stable oxidation products where the level of oxidation at the reactive residues is influenced by the accessibility of their side-chains to the bulk solvent. The aromatic and sulphur-containing residues have been found to react preferentially in accord with previous peptide studies. The sites of oxidation have been determined by tandem mass spectrometry. The rate of oxidation at these reactive markers has been measured for a number of proteolytic peptides as a function of exposure time based on the relative proportion of modified and unmodified peptide ions detected by mass spectrometry. Oxidation rates correlate closely with a theoretical measure of the accessibility of residue side-chains to the solvent in the native protein structure. This approach can distinguish the relative accessibility of the tryptophan residue side-chains of lysozyme at positions 62 and 123 from each other and all other tryptophan residues, and phenylalanine at position 34 from phenylalanine residues at positions 3 and 38 based upon their rates of oxidation.
机译：据报道，一种新方法结合了同步加速器辐射分解和质谱技术来探测蛋白质的结构。使用同步加速器光对蛋白质溶液进行辐射分解后产生的羟基自由基会在毫秒级的时间尺度上修饰氨基酸侧链。这导致形成稳定的氧化产物，其中反应性残基处的氧化水平受其侧链与本体溶剂的可及性影响。已经发现，根据先前的肽研究，芳族和含硫的残基优先反应。氧化位点已通过串联质谱法确定。已经根据质谱法检测到的修饰和未修饰肽离子的相对比例，测量了许多蛋白水解肽在这些反应性标记上的氧化速率与暴露时间的关系。氧化速率与天然蛋白质结构中残基侧链对溶剂可及性的理论测量值密切相关。该方法可以基于它们的氧化速率，将62和123位的溶菌酶色氨酸残基侧链与所有其他色氨酸残基以及34位的苯丙氨酸的相对可及性与3和38位的苯丙氨酸残基彼此区分。

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