Pub. Date : 2008 Apr 22
PMID : 18373354
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Glu162 in homotetrameric human MnSOD spans a dimeric interface and forms a hydrogen bond with His163 of an adjacent subunit which is a direct ligand of the manganese. | Hydrogen | superoxide dismutase 2 | Homo sapiens |
| 2 | The X-ray crystal structures of E162D and E162A MnSOD reveal no significant structural changes compared with the wild type other than the removal of the hydrogen bond interaction with His163 in E162A MnSOD. | Hydrogen | superoxide dismutase 2 | Homo sapiens |
| 3 | In the case of E162D MnSOD, an intervening solvent molecule fills the void created by the mutation to conserve the hydrogen bond interaction between His163 and residue 162. | Hydrogen | superoxide dismutase 2 | Homo sapiens |
| 4 | Differential scanning calorimetry indicates that the hydrogen bond between Glu162 and His163 contributes to the stability of MnSOD, with the major unfolding transition occurring at 81 degrees C for E162A compared to 90 degrees C for wild-type MnSOD. | Hydrogen | superoxide dismutase 2 | Homo sapiens |
| 5 | Differential scanning calorimetry indicates that the hydrogen bond between Glu162 and His163 contributes to the stability of MnSOD, with the major unfolding transition occurring at 81 degrees C for E162A compared to 90 degrees C for wild-type MnSOD. | Hydrogen | superoxide dismutase 2 | Homo sapiens |