Cary P D, Crane-Robinson C, Bradbury E M, Javaherian K, Goodwin G H, Johns E W
Eur J Biochem. 1976 Mar 1;62(3):583-90. doi: 10.1111/j.1432-1033.1976.tb10193.x.
The conformational properties of two non-histone chromosomal proteins (high-mobility-group proteins 1 and 2) have been studied by spectroscopic methods. The interaction of high-mobility-group protein 1 with DNA has also been studied. 1. Circular dichroism results indicate that in the presence of salt both proteins are 40-50% helical between pH 1 and 9. Above pH 9 denaturation takes place. In the absence of salt the proteins denature below pH 4. 2. Nuclear magnetic resonance spectra show the presence of ring-current shifted peaks and perturbed aromatic resonances, demonstrating that the helix formation is accompanied by specific tertiary folding. 3. Nuclear magnetic resonance spectra of compelxes between high mobility group protein 1 and DNA demonstrate that a low ionic strength a portion of the molecule rich in lysine and containing all the aromatic residues is bound to DNA, whilst a more acidic region of the chain remains free from the DNA.
利用光谱学方法研究了两种非组蛋白染色体蛋白（高迁移率族蛋白1和2）的构象特性。同时也研究了高迁移率族蛋白1与DNA的相互作用。1. 圆二色性结果表明，在有盐存在的情况下，两种蛋白在pH值1至9之间40%-50%呈螺旋结构。pH值高于9时发生变性。在无盐情况下，蛋白在pH值低于4时变性。2. 核磁共振谱显示存在环电流位移峰和受扰芳香族共振，表明螺旋结构的形成伴随着特定的三级折叠。3. 高迁移率族蛋白1与DNA复合物的核磁共振谱表明，在低离子强度下，分子中富含赖氨酸且含有所有芳香族残基的一部分与DNA结合，而链中酸性更强的区域则不与DNA结合。
