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Figure 2 | BMC Structural Biology

Figure 2

From: Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold type

Figure 2

Amino acid propensities for exposed and buried residues. Box plots of Amino acid propensities for each SCOP fold for exposed (A) and buried (B) residues in α-helices and for exposed (C) and buried (D) residues in β-strands. The propensities for β-strands for Trp in the “PH domain-like barrel” SCOP fold and for Lys in the “Protein kinase-like” SCOP fold were out of range (4.3 in C and 3.8 in D, respectively) and are not shown. Underlining of certain residues on the horizontal axis denotes that the results from the Fisher-Irwin population proportion test indicated that differences in propensities are statistically significant between folds.

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