Table 2

Electronic properties of amino acid side chains.

pKaa

σI

HMΔPH

σR

σα

σF

AI

HNNMRb


P

10.60

0

0.10

0.10

-0.04

0.02c

0

-

C

10.28

-0.01

-0.01

0.01

-0.03

0.06c

0.01

8.18

A

9.69

0.05

0.05

0

-0.01

0.05

0.05

8.12

I

9.68

0.06

0.08

0.02

-0.04

0.04

0.06

7.99

E

9.67

0.68

1.25

0.57

-0.04

-1.14

0.68

8.40

V

9.62

0.01

0.09

0.08

-0.03

-0.04

0.01

8.08

L

9.60

0.02

0.07

0.05

-0.04

-0.03

0.02

7.99

D

9.60

0.51

1.80

1.29

-0.03

-1.77

0.51

8.38

G

9.60

0

0

0

0

0

0

8.36

W

9.39

0.06

0.15

0.09

-0.12

-0.24

0.06

8.03

M

9.21

0.08

-0.04

-0.12

-0.05

-0.30

0.08

8.12

H

9.17

-0.01

0.21

0.22

-0.06

-0.58

0.01

8.36

S

9.15

-0.03

-0.05

-0.02

-0.02

-0.38

0.03

8.30

F

9.13

0.04

0.06

0.02

-0.08

-0.45

0.04

7.93

Q

9.13

-0.10

-0.07

0.03

-0.05

-0.35

0.10

8.19

Y

9.11

0.05

0.02

-0.03

-0.09

-0.42

0.05

8.10

T

9.10

-0.05

-0.03

0.02

-0.03

-0.44

0.05

8.17

R

9.04

-0.26

-0.75

-0.49

-0.08

0.27

0.26

8.23

K

8.95

-0.16

-1.11

-0.95

-0.05

0.51

0.16

8.29

N

8.80

-0.14

-0.20

-0.06

-0.04

-0.56

0.24

8.33


aThe pKa data were taken from Edsall [58]. bThe HNNMR data were derived from the NMR work of Wishart et al. [32] and represent chemical shift values in p.p.m. for the amide proton of residues in the coil conformation. The other terms have been defined in the text. cEstimated on the basis of chemically similar groups due to anomalous pKa.

Dwyer BMC Chemical Biology 2005 5:2   doi:10.1186/1472-6769-5-2

Open Data