Human linker histone H1 plays a seminal role in eukaryotic DNA packaging. H1 has a tripartite structure consisting of a central, conserved globular domain, which adopts a winged-helix fold, flanked by two variable N- and C-terminal domains. Here we present the backbone resonance assignments of the N-terminal domain and globular domain of human linker histone H1x in the presence and absence of the secondary structure stabilizer sodium perchlorate. Analysis of chemical shift changes between the two conditions is consistent with induction of transient secondary structural elements in the N-terminal domain of H1x in high ionic strength, which suggests that the N-terminal domain adopts significant alpha-helical conformations in the presence of DNA.

中文翻译：

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存在和不存在高氯酸盐时人类接头组蛋白 H1x N 端结构域和球状结构域的 NMR 分配。

人类接头组蛋白 H1 在真核 DNA 包装中起着重要作用。H1 具有三方结构，由中央、保守的球状结构域组成，采用翼状螺旋折叠，两侧是两个可变的 N 和 C 端结构域。在这里，我们展示了在二级结构稳定剂高氯酸钠存在和不存在的情况下，人类接头组蛋白 H1x 的 N 端结构域和球状结构域的骨架共振分配。两种条件之间化学位移变化的分析与在高离子强度下 H1x N 端结构域中瞬时二级结构元件的诱导一致，这表明 N 端结构域在 DNA 存在下采用显着的 α 螺旋构象.