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. Author manuscript; available in PMC: 2016 May 19.
Published in final edited form as: Curr Protoc Bioinformatics. 2015 Dec 17;52:5.8.1–5.815. doi: 10.1002/0471250953.bi0508s52

Figure 5.8.3.

Figure 5.8.3

The submitted sequence and predicted secondary structure and solvent accessibility. The sequence submitted, consisting of 122 residues, is listed at the top of the figure. The predicted secondary structure shown at the middle suggests that this protein is an alpha-beta protein, which contains three alpha-helices (in red) and four beta-strands (in blue). “H,” “S,” and “C” indicate helix, strand, and coil, respectively. The predicted solvent accessibility at the bottom is presented in 10 levels, from buried (0) to highly exposed (9).