Teaching noncovalent interactions in the biochemistry curriculum through molecular visualization:: The search for π interactions
Teaching noncovalent interactions in the biochemistry curriculum through molecular visualization:: The search for π interactions
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DOI：
10.1021/ed077p1424
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发表时间：
2000-11-01
影响因子：
3
通讯作者：
Cox, JR
中科院分区：
文献类型：
--
作者：
Cox, JR
教授学生蛋白质如何采取稳定的三维结构是生物化学课程的主要目标。这个任务的本质是引入氨基酸的结构和各种类型的非共价相互作用。当这两个主题一起教授时，学生们对非共价相互作用在稳定蛋白质和蛋白质复合物结构中的重要性有了更好的认识。生物化学教科书没有认识到芳香族氨基酸参与与其他氨基酸的π相互作用的能力以及这些相互作用在蛋白质稳定性中的作用。为了介绍这些想法，学生们使用分子可视化程序RasMol来搜索各种蛋白质结构中非共价相互作用的具体例子。学生们发现了传统弱相互作用的例子，以及涉及芳香族氨基酸的稳定相互作用的例子。本报告介绍了这些互动，可在随附的网站上查看。这项工作清楚地表明，π型相互作用有助于稳定许多蛋白质的结构和复合物，这种相互作用应纳入生物化学课程。
Teaching students how proteins adopt a stable three-dimensional structure is a major goal in the biochemistry curriculum. Inherent in this task is the introduction of the structure of the amino acids and the various types of noncovalent interactions. When these two topics are taught together, the students gain a better appreciation for the importance of noncovalent interactions in stabilizing the structure of proteins and protein complexes. Biochemistry textbooks have not recognized the ability of aromatic amino acids to participate in π interactions with other amino acids and the role of these interactions in protein stability. To introduce these ideas, RasMol, a molecular visualization program, was used by students to search for specific examples of noncovalent interactions in a variety of protein structures. The students found examples of the traditional weak interactions as well as examples of stabilizing interactions involving aromatic amino acids. These interactions are described in this report and can be viewed at an accompanying Web site. This work clearly demonstrates that π-type interactions help stabilize the structure and complexes of many proteins and that such interactions should be integrated into the biochemistry curriculum.