Figure 2From: Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold typeAmino 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.Back to article page