Abercrombie B D, Kneale G G, Crane-Robinson C, Bradbury E M, Goodwin G H, Walker J M, Johns E W
Eur J Biochem. 1978 Mar;84(1):173-7. doi: 10.1111/j.1432-1033.1978.tb12154.x.
The conformation of the non-histone chromatin protein, HMG 17, has been studied using circular dichroism, infrared and nuclear magnetic resonance spectroscopies, and by small-angle scattering. The results show that in free solution this protein has little or no secondary or tertiary structure in contrast to the other high-mobility-group proteins, HMG 1 and 2, which exhibit highly ordered structures. Protein HMG 17 binds to calf thymus DNA in an ionic-dependent manner, precipitating the DNA at high protein/DNA ratio. The nuclear magnetic resonance data suggest that the principle DNA-binding segment of HMG 17 is that between about residues 15 and 40.
已使用圆二色性、红外光谱和核磁共振光谱以及小角散射研究了非组蛋白染色质蛋白HMG 17的构象。结果表明，与其他具有高度有序结构的高迁移率族蛋白HMG 1和HMG 2相比，该蛋白在游离溶液中几乎没有二级或三级结构。蛋白HMG 17以离子依赖的方式与小牛胸腺DNA结合，在高蛋白/DNA比例下使DNA沉淀。核磁共振数据表明，HMG 17的主要DNA结合片段位于约15至40个残基之间。
