Ronda Luca, Bruno Stefano, Viappiani Cristiano, Abbruzzetti Stefania, Mozzarelli Andrea, Lowe Kenneth C, Bettati Stefano
Department of Biochemistry and Molecular Biology, University of Parma, Italy.
Protein Sci. 2006 Aug;15(8):1961-7. doi: 10.1110/ps.062272306. Epub 2006 Jul 5.
The relative contributions to changes in visible and near UV circular dichroism spectra of hemoglobin of heme ligation and tertiary and quaternary conformational transitions were separated by exploiting the slowing down of structural relaxations for proteins encapsulated in wet, nanoporous silica gels. Spectral signatures, previously assumed to be characteristic of T and R quaternary states, were demonstrated to be specific to different tertiary conformations. The results support the view that ligation and allosteric effectors can modulate the structural and functional properties of hemoglobin by regulating the equilibrium between the same tertiary species within both quaternary states.
通过利用包裹在湿的纳米多孔硅胶中的蛋白质结构弛豫的减慢,分离了血红素连接以及三级和四级构象转变对血红蛋白可见和近紫外圆二色光谱变化的相对贡献。先前被认为是T态和R态四级结构特征的光谱特征,被证明是不同三级构象所特有的。这些结果支持了这样一种观点,即配体结合和变构效应剂可以通过调节两种四级结构中相同三级结构物种之间的平衡来调节血红蛋白的结构和功能特性。