Research Article
Causal Enzymology and Physiological Aspects May Be Accountable to Membrane Integrity in Response to Salt Stress in Arabidopsis thaliana Lines
Table 7
Comparative analysis of residues involved in the dehydrin interactions with the thioesterase.
| | | Name | Distance (Å) | Category | Types | Atomic contact energy (kcal/mol) | Interface area | | (Å2) |
| | Thioesterase | LYS75:NZ -:ASP15:OD2 | 3,29782 | Electrostatic | Attractive Charge | -69.96 | 1132 | | LYS82:NZ -:ASP46:OD1 | 4,76722 | Electrostatic | Attractive Charge | | :ARG221:NH1 -:ILE81:O | 3,37488 | Hydrogen Bond | Conventional Hydrogen Bond | | LYS84:NZ -:SER8:O | 3,29526 | Hydrogen Bond | Conventional Hydrogen Bond | | LYS84:NZ -:LYS82:O | 3,3014 | Hydrogen Bond | Conventional Hydrogen Bond | | :GLY16:CA -:GLY76:O | 2,54704 | Hydrogen Bond | Carbon Hydrogen Bond | | SER79:CB -:GLU79:OE1 | 3,21836 | Hydrogen Bond | Carbon Hydrogen Bond | | ARG10 -:ILE81 | 4,6834 | Hydrophobic | Alkyl | | ALA76 -:ILE81 | 5,04247 | Hydrophobic | Alkyl | | PHE18 -:LYS78 | 4,68931 | Hydrophobic | Pi-Alkyl |
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