Wenxiang diagram

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The wenxiang diagram, also known as the wenxiang graph, was proposed in 1997 by Kuo-Chen Chou (周国城), Chun-Ting Zhang (张春霆), and Gerald M. Maggiora for helping intuitively analyze the disposition of amphiphilic alpha helices in heteropolar environments[1] It is closely related to the earlier 2D diagram called a "helical wheel",[2] which is a slightly idealized projection of the Calphas down the helix axis, also with one-letter-code labels and color-coded symbols to show the sequence and its properties. This diagram is named after the mosquito coil (Chinese: 蚊香; pinyin: wénxiāng), a coiled incense for repelling mosquitos, because of its similar shape. It is a very interesting addition to the general Graph theory in enzymatic kinetics.

Example of wenxiang diagram for a 7-turn amphipathic helix with hydrophobic residues in red and its hydrophilic in blue (generated by the Wenxiang server)

Because the wenxiang diagram is generated by a conical projection of a helix onto a plane, with the start (N-terminus) of the helix at the edge and the end toward the center, the location of each residue in a helix is not only defined by an angle around the diagram’s center, but is also defined by its radius from the center of the diagram in number of turns, which corresponds to its distance along the helix, in number of turns. Therefore, in principle, the wenxiang diagram can be used to represent an alpha-helix of any length.

Wenxiang diagrams have been used to study helix-helix interactions[3] and protein-protein interactions.[4][5] In addition to the Wenxiang server, the helixvis package for the R programming language can also be used to generate Wenxiang graphs.[6]

See also

References

  1. "Disposition of amphiphilic helices in heteropolar environments". Proteins 28 (1): 99–108. May 1997. doi:10.1002/(SICI)1097-0134(199705)28:1<99::AID-PROT10>3.0.CO;2-C. PMID 9144795. 
  2. "Use of helical wheels to represent the structures of proteins and to identify segments with helical potential". Biophys. J. 7 (2): 121–35. March 1967. doi:10.1016/S0006-3495(67)86579-2. PMID 6048867. Bibcode1967BpJ.....7..121S. 
  3. Kurochkina N (May 2010). "Helix-helix interactions and their impact on protein motifs and assemblies". J. Theor. Biol. 264 (2): 585–92. doi:10.1016/j.jtbi.2010.02.026. PMID 20202472. 
  4. Zhou GP (June 2011). "The disposition of the LZCC protein residues in wenxiang diagram provides new insights into the protein-protein interaction mechanism". J Theor Biol 284 (1): 142–8. doi:10.1016/j.jtbi.2011.06.006. PMID 21718705. 
  5. Zhou GP (2011). "The Structural Determinations of the Leucine Zipper Coiled-Coil Domains of the cGMP-Dependent Protein Kinase I alpha and its Interaction with the Myosin Binding Subunit of the Myosin Light Chains Phosphase". Protein & Peptide Letters 18 (10): 966–978. doi:10.2174/0929866511107010966. PMID 21592084. 
  6. Wadhwa, R; Subramanian, V; Stevens-Truss, R (2018). "Visualizing alpha-helical peptides in R with helixvis". Journal of Open Source Software 3 (31): 1008. doi:10.21105/joss.01008. https://CRAN.R-project.org/package=helixvis.