Automated resonance assignment of proteins using heteronuclear 3D NMR .2. Side chain and sequence-specific assignment
Automated resonance assignment of proteins using heteronuclear 3D NMR .2. Side chain and sequence-specific assignment
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DOI：
10.1021/ci960372k
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发表时间：
1997-05-01
期刊：
影响因子：
--
通讯作者：
Sanctuary, BC
中科院分区：
文献类型：
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作者：
Li, KB;Sanctuary, BC
使用异相3D NMR开发了蛋白质的顺序分配方案。该协议由一个氨基酸类型识别算法和一个初级序列映射算法。前者测量每个检测到的自旋模式与20个标准氨基酸偶联模式之间的相似性。考虑了化学位移和拓扑相似性。该映射算法利用氨基酸类型信息将检测到的多肽引导到蛋白质一级序列上的适当位置。分配协议可以应用于由许多不同方法产生的自旋系统。我们设计了几个计算机程序来推导蛋白质的主链和侧链的自旋系统，使用异序3D NMR。然后将结果输入顺序分配方案。所有的算法进行了测试的NMR数据的90个残基的N-结构域的鸡骨骼肌钙蛋白-C。
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures the similarity between each detected spin pattern and 20 standard amino acid coupling patterns. Both chemical shift and topologically likeness are considered. The mapping algorithm uses the amino acid type information to direct detected polypeptides to proper position onto protein primary sequence. The assignment protocol can be applied to spin systems generated by many different approaches. We designed a few computer programs to derive a protein's backbone and side chain spin systems using heteronuclear 3D NMR. The results was then input to the sequential assignment protocol. All of the algorithms were tested on NMR data of a 90-residue N-domain of chicken skeletal troponin-C.