Table 1.

A comparison of structural parameters for PLs adapted to various thermal environments

	Cp	An	Ec	Tt	St	(Meso)	(Thermo)
# of amino acidsa	470.0	484.0	472.0	420.0	432.0	478 ± 6	426 ± 6
Proline content (%)	4.0	7.2	5.5	10.0	4.4	6.4 ± 0.9	7 ± 3
Arginine content (%)	4.7	6.4	7.2	11.7	7.6	6.8 ± 0.4	10 ± 2
Non-polar residues (%)a	53.4	57.4	55.1	62.8	40.7	56.3 ± 1.2	52 ± 11
Polar residues (%)a	46.6	42.5	44.9	37.1	28.9	43.7 ± 1.2	33 ± 4
Charged residues (%)a	25.9	21.9	25.2	30.2	30.3	23.6 ± 1.7	30.3 ± 0.1
# of salt bridgesb	4.3	8.3	6.8	9.3	10.6	7.6 ± 0.8	10.0 ± 0.7
# of surface ion pairsc	6.4	4.5	6.6	10.5	11.6	5.6 ± 1.1	11.1 ± 0.6
TSASAa (Å2)	22,833	20,372	20,306	18,555	18,305	20,339 ± 33	18,430 ± 125
TSASA/residue	48.6	42.1	43.0	44.2	42.4	42.6 ± 0.5	43.3 ± 0.9
CHASAb (Å2)	10,159	7587	7302	7220	7083	7445 ± 143	7152 ± 69
CHASA/residue	21.6	15.7	15.5	17.2	16.4	15.6 ± 0.1	16.8 ± 0.4
% CHASA/TSASA	44.5	37.2	36.0	38.9	38.7	36.6 ± 0.6	38.8 ± 0.1
% per residue	2.3	2.7	2.8	2.6	2.6	2.8 ± 0.1	2.6

TSASA total solvent accessible surface area, CHASA conditional hydrophobic accessible surface area. See text for referencing

^aProtParam tool

^bESBRI

^cProtein interactions calculator