The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.
The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.
复制标题
埋藏极性基团对 GCN4 卷曲线圈构象稳定性的贡献。
DOI：
10.1006/jmbi.2000.3936
复制
发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Hu,JC
中科院分区：
文献类型：
--
作者：
Zhu,H;Celinski,SA;Scholtz,JM;Hu,JC
来自GCN 4的亮氨酸拉链卷曲螺旋的二聚体界面已被用于探测疏水和氢键相互作用对蛋白质稳定性的贡献。我们已经确定了将Ile或Asn残基放置在双链卷曲螺旋中的四个埋藏位置的能量。正如预期的那样，Ile在这些掩埋位置比Asn更受青睐，但不像仅考虑疏水效应所预测的那样多。看来，链间氢键之间形成的侧链之间的掩埋的天冬酰胺残基，这些有助于卷曲螺旋肽的构象稳定性。然而，这些贡献高度依赖于Asn对的位置。Ile到Asn突变的影响在肽的N末端最大，并且当我们将取代从N末端移动到C末端七肽时几乎降低两倍。
The dimeric interface of the leucine zipper coiled coil from GCN4 has been used to probe the contributions of hydrophobic and hydrogen bonding interactions to protein stability. We have determined the energetics of placing Ile or Asn residues at four buried positions in a two-stranded coiled coil. As expected, Ile is favored over Asn at these buried positions, but not as much as predicted by considering only the hydrophobic effect. It appears that interstrand hydrogen bonds form between the side-chains of the buried Asn residues and these contribute to the conformational stability of the coiled-coil peptides. However, these contributions are highly dependent on the locations of the Asn pairs. The effect of an Ile to Asn mutation is greatest at the N terminus of the peptide and decreases almost twofold as we move the substitution from the N to C-terminal heptads.