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Table 2 Mean amino acid propensities for α-helix and β-strand conformations

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

Amino acid α-helix β-strand
  Exposed residues Buried residues Total residues Exposed residues Buried residues Total residues
V 0.83 0.89 0.91 2.31 1.57 2.00
I 0.96 1.01 1.04 2.02 1.39 1.79
L 1.16 1.27 1.28 1.18 0.93 1.15
M 1.03 1.29 1.26 1.01 0.84 1.01
P 0.48 0.41 0.44 0.49 0.42 0.40
A 1.43 1.37 1.41 0.48 0.72 0.75
C 0.63 0.85 0.85 1.24 1.07 1.36
F 0.88 0.99 1.00 1.50 1.10 1.4
Y 0.91 0.98 0.98 1.71 1.12 1.37
W 0.87 1.09 1.07 1.90 0.91 1.23
Q 1.34 1.21 1.26 0.96 0.82 0.72
S 0.74 0.80 0.76 0.86 0.85 0.81
T 0.72 0.84 0.78 1.58 1.08 1.21
N 0.74 0.77 0.73 0.71 0.76 0.63
H 0.90 0.85 0.87 1.15 0.98 0.99
D 0.91 0.73 0.82 0.61 0.76 0.55
K 1.25 1.13 1.17 1.14 0.98 0.76
E 1.51 1.25 1.39 0.89 0.86 0.65
R 1.31 1.13 1.21 1.27 0.82 0.85
G 0.28 0.59 0.44 0.41 0.81 0.67