Table 2

ΔASA in the SALTIN and OSMOL samples.

SALTIN

HALOPHILES

NON

HALOPHILES

ΔApAa)

ΔTot Ob)

ΔSc Oc)

ΔTot Nd)

ΔSc Ne)

OSMOL

HALOPHILES

NON

HALOPHILES

ΔApAa)

ΔTot Ob)

ΔSc Oc)

ΔTot Nd)

ΔSc Ne)


1DOI

1FXA

-0.07

0.06

-0.08

0.01

0.01

1NWZ

1MZU

-0.05

0.08

0.05

-0.03

-0.02

1TJO

2VXX

-0.09

0.14

0.15

-0.04

-0.04

3IBM

3KGZ

-0.07

0.02

0.02

0.04

0.04

2CC6

2V18

-0.07

0.17

0.15

-0.10

-0.09

1CNO

1ETP

-0.02

0.00

0.01

0.01

0.02

1ITK

2FXG

-0.10

0.13

0.14

-0.03

-0.03

2VPN

3FXB

-0.06

0.06

0.05

-0.01

-0.00

2AZ3

3B54

-0.02

0.09

0.08

-0.06

-0.06

3BSM

2QJJ

0.00

0.00

0.00

0.01

0.01

3IFV

1RWZ

-0.03

0.07

0.08

-0.04

-0.03


Totalf)

-0.38

0.66

0.52

-0.28

-0.25

-0.21

0.16

0.14

0.02

0.05

Averageg)

-0.06

0.11

0.90

-0.05

-0.04

-0.04

0.03

0.03

0.00

0.01

t-testh)

0.00

0.00

0.05

0.02

0.03

0.03

0.11

    0.07

0.71

0.42

Wilcoxonh)

0.03

0.03

0.05

0.05

0.05

0.04

0.14

0.04

0.50

0.50


Differences of fractional accessibility surface area (ΔASA) in the SALTIN and OSMOL samples for different class of atoms. The differences are between the surface areas calculated in the halophilic protein and the corresponding areas in the non-halophilic counterpart. The calculations were performed considering the proteins in their quaternary structure.

a) Apolar ΔASA difference between fractional apolar exposed areas of the halophilic protein and the corresponding non-halophilic homolog

b) Oxygen atom fractional ΔASA

c) Side-chain oxygen atom fractional ΔASA

d) Nitrogen atom fractional ΔASA

e) Side-chain nitrogen fractional ΔASA

f) Total fractional ΔASA

g) Average fractional ΔASA

h) Boldfaced and underlined p-values indicate significant or possible trend, respectively

Siglioccolo et al. BMC Structural Biology 2011 11:50   doi:10.1186/1472-6807-11-50

Open Data