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

BMC Structural Biology

Table 4 Number of CHCs found in the two samples with the corresponding Δ ACA.

SALTIN HALOPHILE	Seq. lenght	NON HALOPHILE	Seq. lenght	Sequence identity(%)	No. CHC	OSMOL HALOPHILE	Seq. lenght	NON HALOPHILE	Seq. lenght	Sequence identity(%)	No. CHC
1DOI	128	1FXA	98	51	50	1NWZ	125	1MZU	129	46	55
1TJO	182	2VXX	192	36	36	1CNO	87	1ETP	190	44	26
2B5W	357	2CD9	366	30	154	1NML	326	3HQ6	345	47	157
2CC6	68	2V18	68	42	33	2VPN	316	3FXB	326	64	132
1ITK	731	2FXG	748	60	514	3IGN	177	3I5C	206	62	63
2AZ3	164	3B54	161	54	71	3BSM	413	2QJJ	402	40	187
2J5K	304	1Y6J	318	33	101	3IBM	167	3KGZ	156	66	65
3IFV	247	1RWZ	245	36	104
Total^a)					329.33						58.56
Average^b)					-0.31						-0.08
t-test^c)					0.03						0.52
Wilcoxon^c)					0.01						0.63

Number of conserved hydrophobic contacts (CHCs) found in the two samples and the corresponding overall difference of apolar contact area (Δ ACA)
a) Total Δ ACA in the CHCs
b) Average Δ ACA in the CHCs
c) Boldfaced digits indicate significant p-values

ISSN: 1472-6807