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

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

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       
Totala)      329.33       58.56
Averageb)      -0.31       -0.08
t-testc)      0.03       0.52
Wilcoxonc)      0.01       0.63
  1. Number of conserved hydrophobic contacts (CHCs) found in the two samples and the corresponding overall difference of apolar contact area (Δ ACA)
  2. a) Total Δ ACA in the CHCs
  3. b) Average Δ ACA in the CHCs
  4. c) Boldfaced digits indicate significant p-values