Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions.
Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions.
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DOI：
10.1042/bst0380861
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发表时间：
2010-08
影响因子：
3.9
通讯作者：
B. Wallace;R. W. Janes
中科院分区：
文献类型：
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作者：
B. Wallace;R. W. Janes
CD（圆二色性）光谱是结构生物学中的一种成熟技术。SRCD（同步辐射圆二色性）光谱扩展了传统CD光谱（使用实验室仪器）的实用性和应用，因为同步加速器的高通量能够在较低波长下收集数据（导致更高的信息含量），检测具有更高信噪比水平的光谱，并在存在吸收成分（缓冲液，盐，脂质和洗涤剂）的情况下进行测量。SRCD光谱可以提供重要的静态和动态的蛋白质在溶液中的结构信息，包括完整的蛋白质和它们的结构域的二级结构，蛋白质的稳定性，野生型和突变型蛋白质之间的差异，在蛋白质中的天然无序区域的识别，以及蛋白质折叠和膜插入的动态过程和酶反应的动力学。它也被用于有效地研究蛋白质相互作用，包括蛋白质-蛋白质复合物的形成，涉及诱导配合或刚体机制，以及蛋白质-脂质复合物。一个新的基于网络的生物信息学资源，蛋白质圆二色性数据库（PCDDB），已经创建，使存档，访问和分析CD和SRCD光谱和支持元数据，现在使这一信息公开。总之，发展中的方法SRCD光谱有可能在蛋白质构象及其复合物的新型研究中发挥重要作用。
CD (circular dichroism) spectroscopy is a well-established technique in structural biology. SRCD (synchrotron radiation circular dichroism) spectroscopy extends the utility and applications of conventional CD spectroscopy (using laboratory-based instruments) because the high flux of a synchrotron enables collection of data at lower wavelengths (resulting in higher information content), detection of spectra with higher signal-to-noise levels and measurements in the presence of absorbing components (buffers, salts, lipids and detergents). SRCD spectroscopy can provide important static and dynamic structural information on proteins in solution, including secondary structures of intact proteins and their domains, protein stability, the differences between wild-type and mutant proteins, the identification of natively disordered regions in proteins, and the dynamic processes of protein folding and membrane insertion and the kinetics of enzyme reactions. It has also been used to effectively study protein interactions, including protein-protein complex formation involving either induced-fit or rigid-body mechanisms, and protein-lipid complexes. A new web-based bioinformatics resource, the Protein Circular Dichroism Data Bank (PCDDB), has been created which enables archiving, access and analyses of CD and SRCD spectra and supporting metadata, now making this information publicly available. To summarize, the developing method of SRCD spectroscopy has the potential for playing an important role in new types of studies of protein conformations and their complexes.