Cooperative hydrogen bonding effects are key determinants of backbone amide proton chemical shifts in proteins
Cooperative hydrogen bonding effects are key determinants of backbone amide proton chemical shifts in proteins
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DOI：
10.1021/ja0617901
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发表时间：
2006-08-02
影响因子：
15
通讯作者：
Jensen, Jan H.
中科院分区：
文献类型：
--
作者：
Parker, Laura L.;Houk, Andrew R.;Jensen, Jan H.
本文提出了一种基于量子力学从头计算方法对部分蛋白质骨架酰胺质子化学位移（δ（H））进行预测的方法。该方法用于预测和解释蛋白G和泛素中的13个δ（H）值。预测的酰胺-酰胺δ（H）值在实验的0.6 ppm内，均方根偏差（RMSD）为0.3 ppm。我们发现，虽然氢键的几何形状是最重要的δ（H）-决定因素，扩展的氢网络的长程合作效应作出显着贡献的δ（H）。我们提出了一个简单的模型，准确地将蛋白质结构与delta（H）联系起来。
A computational methodology for backbone amide proton chemical shift (delta(H)) predictions based on ab initio quantum mechanical treatment of part of the protein is presented. The method is used to predict and interpret 13 delta(H) values in protein G and ubiquitin. The predicted amide-amide delta(H) values are within 0.6 ppm of experiment, with a root-mean-square deviation (RMSD) of 0.3 ppm. We show that while the hydrogen bond geometry is the most important delta(H)-determinant, longer-range cooperative effects of extended hydrogen networks make significant contributions to delta(H). We present a simple model that accurately relates the protein structure to delta(H).