Zhu Fujiang, Isaacs Neil W, Hecht Lutz, Barron Laurence D
WestCHEM, Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Structure. 2005 Oct;13(10):1409-19. doi: 10.1016/j.str.2005.07.009.
On account of its sensitivity to chirality, Raman optical activity (ROA), measured here as the intensity of a small, circularly polarized component in the scattered light using unpolarized incident light, is a powerful probe of protein structure and behavior. Protein ROA spectra provide information on secondary and tertiary structures of polypeptide backbones, backbone hydration, and side chain conformations, and on structural elements present in unfolded states. This article describes the ROA technique and presents ROA spectra, recorded with a commercial instrument of novel design, of a selection of proteins to demonstrate how ROA may be used to readily distinguish between the main classes of protein structure. A principal component analysis illustrates how the many structure-sensitive bands in protein ROA spectra are favorable for applying pattern recognition techniques to determine structural relationships between different proteins.
由于其对手性的敏感性，拉曼光学活性（ROA）在此处被测量为使用非偏振入射光时散射光中一个小的圆偏振分量的强度，它是蛋白质结构和行为的有力探测手段。蛋白质ROA光谱提供了关于多肽主链的二级和三级结构、主链水合作用以及侧链构象的信息，以及关于未折叠状态下存在的结构元件的信息。本文描述了ROA技术，并展示了用新型设计的商业仪器记录的一系列蛋白质的ROA光谱，以说明如何使用ROA轻松区分蛋白质结构的主要类别。主成分分析说明了蛋白质ROA光谱中许多对结构敏感的谱带如何有利于应用模式识别技术来确定不同蛋白质之间的结构关系。
