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首页> 外文期刊>Journal of Molecular Biology >The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.
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The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.

机译：埋藏的极性基团对GCN4盘绕线圈构象稳定性的贡献。

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摘要

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. Copyright 2000 Academic Press.
机译：来自GCN4的亮氨酸拉链盘绕线圈的二聚体界面已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残基放置在两链盘绕线圈中的四个掩埋位置的能量学。不出所料，在这些埋藏位置，Ile比Asn更受青睐，但不如仅考虑疏水作用所预测的那么多。似乎在掩埋的Asn残基的侧链之间形成了链间氢键，并且这些氢键有助于卷曲螺旋肽的构象稳定性。但是，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端最大，并且当我们将取代从N端移到C端七肽时，其影响几乎降低了两倍。版权所有2000学术出版社。

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