Table 2.3: Relative frequencies of amino acid residues in secondary structures

Amino acid

α helix

β sheet

Reverse turn

Glu

1.59

0.52

1.01

Ala

1.41

0.72

0.82

Leu

1.34

1.22

0.57

Met

1.30

1.14

0.52

Gln

1.27

0.98

0.84

Lys

1.23

0.69

1.07

Arg

1.21

0.84

0.90

His

1.05

0.80

0.81

Val

0.90

1.87

0.41

Ile

1.09

1.67

0.47

Tyr

0.74

1.45

0.76

Cys

0.66

1.40

0.54

Trp

1.02

1.35

0.65

Phe

1.16

1.33

0.59

Thr

0.76

1.17

0.96

Gly

0.43

0.58

1.77

Asn

0.76

0.48

1.34

Pro

0.34

0.31

1.32

Ser

0.57

0.96

1.22

Asp

0.99

0.39

1.24

Note: The amino acids are grouped according to their preference for α helices (top group), β sheets (middle group), or turns (bottom group).

Source: T. E. Creighton, Proteins: Structures and Molecular Properties, 2d ed. (W. H. Freeman and Company, 1992), p. 256.