无机盐诱导的肌球蛋白构象变化的激光拉曼光散射观测
Laser Raman light-scattering observations of conformational changes in myosin induced by inorganic salts.
作者信息
Barrett T W, Peticolas W L, Robson R M
出版信息
Biophys J. 1978 Sep;23(3):349-58. doi: 10.1016/S0006-3495(78)85454-X.
The Raman spectra of aqueous solutions of myosin and mixtures of myosin in solutions of the salts CaCl(2), MgCl(2), and LiBr have been taken. The spectrum of the solvent background has been subtracted by means of a computer, leaving only the Raman peaks of the protein. From an analysis of the Raman bands in the regions at 900, 940, 1,240-1,300, and 1,650-1,670 cm(-1), it seems likely that CaCl(2) effects an alpha-to beta-transition in myosin, probably owing to the interaction of the Ca(2+) ion, LiBr appears to denature the protein leading to increased random coil structure, and MgCl(2) appears to have an effect intermediate between the two other salts. These results are reported for concentrations as low as 10(-5) M of CaCl(2) and MgCl(2).This investigation indicates the usefulness of the Raman light-scattering technique for the study of protein conformational changes.
已获取肌球蛋白水溶液以及肌球蛋白在氯化钙、氯化镁和溴化锂溶液中的混合物的拉曼光谱。通过计算机减去了溶剂背景光谱，仅留下蛋白质的拉曼峰。通过对900、940、1240 - 1300和1650 - 1670 cm⁻¹区域的拉曼谱带进行分析，似乎氯化钙会使肌球蛋白发生α到β的转变，这可能是由于Ca²⁺离子的相互作用；溴化锂似乎会使蛋白质变性，导致无规卷曲结构增加；而氯化镁的作用似乎介于另外两种盐之间。这些结果是针对低至10⁻⁵ M的氯化钙和氯化镁浓度报告的。这项研究表明拉曼光散射技术在研究蛋白质构象变化方面的有用性。
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