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Table 2 Δ ASA in the SALTIN and OSMOL samples.

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

SALTIN HALOPHILES NON HALOPHILES Δ ApAa) Δ Tot Ob) Δ Sc Oc) Δ Tot Nd) Δ Sc Ne) OSMOL HALOPHILES NON HALOPHILES Δ ApAa) Δ Tot Ob) Δ Sc Oc) Δ Tot Nd) Δ Sc 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
  1. 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.
  2. a) Apolar Δ ASA difference between fractional apolar exposed areas of the halophilic protein and the corresponding non-halophilic homolog
  3. b) Oxygen atom fractional Δ ASA
  4. c) Side-chain oxygen atom fractional Δ ASA
  5. d) Nitrogen atom fractional Δ ASA
  6. e) Side-chain nitrogen fractional Δ ASA
  7. f) Total fractional Δ ASA
  8. g) Average fractional Δ ASA
  9. h) Boldfaced and underlined p-values indicate significant or possible trend, respectively