STING Contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces
STING Contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces
复制标题
DOI：
10.1093/bioinformatics/bth203
复制
发表时间：
2004-09-01
期刊：
影响因子：
5.8
通讯作者：
Neshich, G
中科院分区：
文献类型：
--
作者：
Mancini, AL;Higa, RH;Neshich, G
氨基酸之间的相互作用是分析蛋白质及其复合体结构时要考虑的重要因素。因此，分子生物学家确实需要特定的工具来识别和可视化所有这些联系。图形接触(GC)和形成残基图形接触的界面(IFRgc)，根据预先定义的原子类型及其距离对的表格计算氨基酸之间的原子接触，然后以不同的形式显示它们。目前由GC和IFRgc列出的接触类型清单包括氢键(九种不同口味)、疏水相互作用、电荷-电荷相互作用、芳香族堆积和二硫键。如此广泛的相互作用目录，代表了支配蛋白质折叠、稳定性和结合的力量，是这两种应用的关键特征。GC和IFRgc是STING Millennium Suite的一部分。
Amino acid contacts in terms of atomic interactions are essential factors to be considered in the analysis of the structure of a protein and its complexes. Consequently, molecular biologists do require specific tools for the identification and visualization of all such contacts. Graphical contacts (GC) and interface forming residue graphical contacts (IFRgc) presented here, calculate atomic contacts among amino acids based on a table of predefined pairs of the atom types and their distances, and then display them using number of different forms. The inventory of currently listed contact types by GC and IFRgc include hydrogen bonds (in nine different flavors), hydrophobic interactions, charge-charge interactions, aromatic stacking and disulfide bonds. Such extensive catalog of the interactions, representing the forces that govern protein folding, stability and binding, is the key feature of these two applications. GC and IFRgc are part of STING Millennium Suite.