Abstract
The wenxiang diagram was proposed to represent α-helices in a 2D (two dimensional) space (Chou, K.C., Zhang, C.T., Maggiora, G.M. Proteins: Struct., Funct., Genet., 1997, 28, 99-108). It has the capacity to provide more information in a 2D plane about each of the constituent amino acid residues in an α-helix, and is particularly useful for studying and analyzing amphiphilic helices. To meet the increasing requests for getting the program of generating wenxiang diagrams, a user-friendly web-server called “Wenxiang” has been established. It is accessible to the public at the web-site http://www.jci-bioinfo.cn/wenxiang2 or http://icpr.jci.edu.cn/bioinfo/wenxiang2. Further- more, for the convenience of users, here we provide a step-to-step guide for how to use the Wenxiang web-server to generate the desired wenxiang diagrams.
Highlights
The α-helix is one of the most basic and fundamental elements in protein structure [1]
For the convenience of users, here we provide a step-to-step guide for how to use the Wenxiang web-server to generate the desired wenxiang diagrams
Α-helices have had an immense influence on our understanding of protein structure
Summary
The α-helix is one of the most basic and fundamental elements in protein structure [1]. 4) Click on the Black & White button to generate a black-and-white wenxiang diagram (Figure 3), where hydrophobic residues are shown by “black-filled circles with white characters” while hydrophilic residues by “open circles with black characters”. It will take about 20 seconds before the desired diagram is completely shown on the screen.
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