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  3. Electron Paramagnetic Resonance

Electron Paramagnetic Resonance电子顺磁共振

释义：

EPR (also called ESR, Electron Spin Resonance) spectroscopy is analogous to NMR, but is based on the excitation of unpaired electrons instead of nuclei. Unpaired (single) electrons are only found in radicals and some metal ions (paramagnetic species); the EPR spectrum provides information about the environment and mobility of the paramagnetic species. The magnetic interaction of two paramagnetic centres in a protein can be used to calculate the distance between them; this allows studies of the movements and interactions of protein segments. In proteins without any intrinsic unpaired electrons it is possible to attach a radical probe (spin label). Stable nitroxide radicals can be bound to amino acid residues, in analogy with fluorescent probes. In combination with site directed mutagenesis this method is used in particular to study structure and assembly of membrane proteins, by measuring with EPR whether an amino acid is in a polar or non polar environment.

电子顺磁共振，EPR (也称为 ESR，电子自旋共振) 光谱学类似于 NMR，但它基于对未配对电子而非原子的激发。未配对 (单个) 电子仅存在于自由基和一些金属离子 (顺磁性物质) 中；EPR 光谱提供了有关顺磁性物质环境和流动性的的信息。蛋白质中两个顺磁中心的磁相互作用可用于计算它们之间的距离；这使得研究蛋白质片段的运动和相互作用成为可能。在没有固有未配对电子的蛋白质中，可以附加自由基探针 (自旋标签)。 稳定的硝基自由基可以结合到氨基酸残基上，类似于荧光探针。结合定点突变技术，这种方法特别用于研究膜蛋白的结构和组装，通过测量 EPR 来确定氨基酸是否处于极性或非极性环境中。

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