Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface

BMC Structural Biology

Table 2 Δ ASA in the SALTIN and OSMOL samples.

SALTIN HALOPHILES	NON HALOPHILES	Δ ApA^a)	Δ Tot O^b)	Δ Sc O^c)	Δ Tot N^d)	Δ Sc N^e)	OSMOL HALOPHILES	NON HALOPHILES	Δ ApA^a)	Δ Tot O^b)	Δ Sc O^c)	Δ Tot N^d)	Δ Sc N^e)
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
Total^f)		-0.38	0.66	0.52	-0.28	-0.25			-0.21	0.16	0.14	0.02	0.05
Average^g)		-0.06	0.11	0.90	-0.05	-0.04			-0.04	0.03	0.03	0.00	0.01
t-test^h)		0.00	0.00	0.05	0.02	0.03			0.03	0.11	0.07	0.71	0.42
Wilcoxon^h)		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 (Δ ASA) 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 Δ ASA difference between fractional apolar exposed areas of the halophilic protein and the corresponding non-halophilic homolog
b) Oxygen atom fractional Δ ASA
c) Side-chain oxygen atom fractional Δ ASA
d) Nitrogen atom fractional Δ ASA
e) Side-chain nitrogen fractional Δ ASA
f) Total fractional Δ ASA
g) Average fractional Δ ASA
h) Boldfaced and underlined p-values indicate significant or possible trend, respectively

ISSN: 1472-6807