FLUORESCENCE ASSISTED INFRARED MICROSPECTROSCOPY TO STUDY OF OSTEOPOROSIS

红外光谱学提供了一种极好的手段 蛋白质的二级结构。酰胺I的去卷积 波段(1600-1700 cm-1)，主要是C=O伸缩模式 形成蛋白质主干的多肽连接提供了详细信息 蛋白质结构中？-螺旋、？-片状的百分比， ？-圈数，或加长线圈。使用灵敏的红外光谱 技术和强大的反卷积方法，如傅立叶自卷积 反褶积和二阶导数分析，红外光谱分析 可以随着展开研究二级结构的详细变化。 以时间分辨的方式研究蛋白质折叠是有益的， 然而，传统的停流混合器的时间限制在 几毫秒，需要相对较大的解 哈沃斯。然而，使用明亮的光源，如激光 H(用于拉曼或荧光光谱)和同步加速器红外光 H(用于FTIR光谱)，显著减少大面积(因此 H卷)，这是必要的。数量级为10？m x的体积元素 H10？m×10？m(~1pl)足以获得高质量的光谱。

Infrared spectroscopy provides an excellent means for examining the secondary structure of proteins. The deconvolution of the Amide I band (1600 - 1700 cm-1), which is primarily a C=O stretching mode of the peptide linkage that forms the protein backbone, provides details of the percent of the protein structure that is ?-helical, ?-sheet, ?-turn, or extended coil. Using sensitive infrared spectroscopic techniques and powerful deconvolution methods such as Fourier self deconvolution and second derivative analysis, infrared spectroscopy can study the detailed changes in secondary structure with unfolding. It is beneficial to study protein folding in a time-resolved fashion, however the time limit of a conventional stopped flow mixers is on the Horder of several milliseconds and requires relatively large solution Hvolumes. However, the use of bright light sources, such as lasers H(for Raman or fluorescence spectra) and synchrotron infrared light H(for FTIR spectra), significantly reduce the large areas (and hence Hvolumes) that are necessary. Volume elements on the order of 10 ?m x H10 ?m x 10 ?m (~1 pl) are sufficient to obtain high quality spectra.