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Table 2 Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms in various architectural contexts.

From: On the evolutionary conservation of hydrogen bonds made by buried polar amino acids: the hidden joists, braces and trusses of protein architecture

 

Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms

Amino Acid

Within helix N-termini

Within helix C-termini

Within edge strands

From edge strands

Within central strands

From central strands

Within 310 helices

Within β-hairpins

Within polyproline helices

Within coil regions

 

Con

All

Con

All

Con

All

Con

All

Con

All

Con

All

Con

All

Con

All

Con

All

Con

All

Arg

1.05

0.46

14.38

6.44

3.17

3.29

1.71

3.25

0.34

1.73

3.07

3.42

3.02

3.52

1.48

2.69

6.11

3.70

2.48

3.52

Asn

1.30

2.88

1.14

1.84

3.12

3.20

3.20

2.00

2.44

2.44

3.06

2.30

1.58

2.41

1.13

3.05

2.54

2.43

1.85

2.57

Asp

4.84

3.04

0.61

0.54

2.65

1.20

2.27

2.06

0.97

1.44

2.42

1.46

3.04

2.28

6.37

2.97

1.74

1.43

5.20

2.52

Cys

9.86

2.20

4.52

1.40

3.83

2.66

0.93

2.22

5.09

4.06

0.39

2.53

8.99

2.59

4.51

1.70

1.55

0.84

5.94

1.97

Gln

0.11

1.22

0.44

1.80

2.33

2.98

6.19

2.23

4.87

1.86

1.67

2.10

0.96

1.69

1.04

1.80

1.55

3.06

0.52

1.96

Glu

1.94

1.40

0.00

0.06

0.00

0.82

0.00

0.64

0.57

0.48

2.35

0.78

0.81

0.79

0.08

0.93

0.80

1.19

0.90

0.99

His

2.37

1.13

0.89

2.50

0.97

2.24

4.08

2.14

0.82

2.08

1.81

2.22

1.45

2.62

1.90

1.89

4.71

2.38

2.66

2.08

Lys

0.00

0.13

0.60

1.99

0.00

1.05

0.00

0.88

1.25

0.51

0.00

1.12

0.15

1.18

0.00

0.67

0.40

1.00

0.13

0.97

Ser

1.53

3.43

0.65

2.15

0.47

1.92

2.61

2.01

2.32

3.22

2.46

1.75

1.09

2.01

3.58

2.23

0.76

2.03

0.90

1.95

Thr

1.53

3.64

0.70

2.05

2.91

1.81

0.68

2.25

3.43

3.29

0.48

2.37

0.65

1.88

0.75

2.23

0.62

1.88

1.19

1.81

Trp

0.81

0.23

0.36

1.28

2.06

1.31

6.53

2.01

1.84

1.83

1.84

1.83

3.41

1.23

3.88

1.40

2.93

1.25

3.58

1.30

Tyr

1.06

0.68

0.56

1.23

4.04

1.77

0.30

2.37

1.03

1.26

3.14

2.37

4.20

1.37

0.07

0.91

3.12

1.84

1.60

1.39

  1. Columns headed "Col" display the propensities of conserved buried polar residues.
  2. Columns headed "All" display the propensities of all polar residues forming the indicated interaction (regardless of solvent accessibility or conservation).