Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK.
Biochem Soc Trans. 2010 Aug;38(4):861-73. doi: 10.1042/BST0380861.
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.
圆二色性（CD）光谱学是结构生物学中一种成熟的技术。同步辐射圆二色性（SRCD）光谱学扩展了常规 CD 光谱学（使用基于实验室的仪器）的应用，因为同步加速器的高通量可以在更低的波长下收集数据（从而产生更高的信息量），检测具有更高信噪比的光谱，并在有吸收成分（缓冲液、盐、脂质和洗涤剂）存在的情况下进行测量。SRCD 光谱学可以提供有关溶液中蛋白质的重要静态和动态结构信息，包括完整蛋白质及其结构域的二级结构、蛋白质稳定性、野生型和突变型蛋白质之间的差异、蛋白质中天然无规区域的鉴定，以及蛋白质折叠和膜插入的动态过程以及酶反应的动力学。它还被用于有效地研究蛋白质相互作用，包括涉及诱导契合或刚体机制的蛋白质-蛋白质复合物形成，以及蛋白质-脂质复合物。创建了一个新的基于网络的生物信息学资源，即蛋白质圆二色性数据库（PCDDB），它可以对 CD 和 SRCD 光谱以及支持元数据进行存档、访问和分析，现在可以公开提供这些信息。总之，SRCD 光谱学的发展方法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。
