Kuptsov A H, Trofimov V I
Institute for biological testing of chemicals, Kupavna, Moscow region, USSR.
J Biomol Struct Dyn. 1985 Aug;3(1):185-96. doi: 10.1080/07391102.1985.10508406.
We have studied dependence of the S-S and C-S raman bands frequencies and intensities on the conformation of disulfide bridges. These correlations have been analyzed on the basis of the normal coordinates treatment in the valence force field and from comparison of the raman and X-ray data for the model compounds and proteins. The found regularity of the intensity variations with conformation make it possible to distinguish these spectral perturbations from those associated with the change in the number of disulfide bridges in proteins. Particularly, this was demonstrated on the gamma-irradiated insulin solutions spectra. We also present some data appropriate for estimation of the content of disulfide bridges in proteins using internal intensity standards.
我们研究了S-S和C-S拉曼谱带频率及强度与二硫键构象的相关性。已根据价键力场中的简正坐标处理方法，并通过比较模型化合物和蛋白质的拉曼数据与X射线数据，对这些相关性进行了分析。所发现的强度随构象变化的规律，使得我们能够将这些光谱扰动与蛋白质中二硫键数量变化相关的扰动区分开来。特别是，这一点在γ辐照胰岛素溶液的光谱中得到了证明。我们还给出了一些适用于使用内部强度标准估算蛋白质中二硫键含量的数据。
