Susi H, Byler D M, Purcell J M
J Biochem Biophys Methods. 1985 Oct;11(4-5):235-40. doi: 10.1016/0165-022x(85)90005-3.
Fourier self-deconvolution was applied to the infrared spectra of five globular proteins with a high beta-structure content and to the essentially alpha-helical protein hemoglobin. The featureless amide I' bands around 1650 cm-1 were thereby resolved into six to nine components, depending on the protein. Specific components were assigned to the beta-structure segments in each protein. The frequencies and the number of 'beta-bands' differ from one protein to another. The areas of the components were evaluated by means of a Gauss-Newton iteration procedure. It appears that the total area of the beta-bands, as a fraction of the total amide I' band area, reflects the relative beta-structure content of each protein studied.
傅里叶自去卷积法被应用于五种具有高β结构含量的球状蛋白质以及本质上为α螺旋结构的蛋白质血红蛋白的红外光谱分析。由此，1650cm-1附近无特征的酰胺I'带被分解为六至九个组分，具体数量取决于蛋白质。特定组分被归属于每种蛋白质中的β结构片段。“β带”的频率和数量因蛋白质而异。通过高斯-牛顿迭代法对各组分的面积进行评估。结果表明，β带的总面积占酰胺I'带总面积的比例反映了所研究的每种蛋白质的相对β结构含量。
