Land M D, Cox D J, Manning D R, Reeck G R
Biochim Biophys Acta. 1985 Oct 4;831(2):207-12. doi: 10.1016/0167-4838(85)90037-8.
HMG-1, HMG-2 and HMG-E were purified from chicken erythrocyte chromatin without exposure to overt denaturing conditions and subjected to several types of physical measurement. The principal conclusions drawn from the measurements were: none of the proteins has a strong tendency to self-associate, although HMG-1 does weakly self-associate; the frictional properties of HMG-1 and HMG-E (and probably HMG-2) indicate that the proteins deviate significantly from compact, moderately hydrated spheres; and each of the proteins contains approximately 40% helix and little if any beta-pleated sheet.
HMG-1、HMG-2和HMG-E是从鸡红细胞染色质中纯化得到的,未暴露于明显的变性条件下,并进行了几种类型的物理测量。从这些测量中得出的主要结论是:尽管HMG-1确实有较弱的自我缔合倾向,但这些蛋白质都没有很强的自我缔合倾向;HMG-1和HMG-E(可能还有HMG-2)的摩擦特性表明,这些蛋白质与紧密的、适度水合的球体有显著偏差;并且每种蛋白质都含有约40%的螺旋结构,几乎没有β-折叠结构。