General Stability | Organism |
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compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations | Haloarcula hispanica |
compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations | Halalkalicoccus jeotgali |
compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations | Haloarcula marismortui |
Organism | UniProt | Comment | Textmining |
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Halalkalicoccus jeotgali | D8J7H2 | - |
- |
Halalkalicoccus jeotgali DSM 18796 | D8J7H2 | - |
- |
Haloarcula hispanica | Q4A3E0 | - |
- |
Haloarcula marismortui | Q5UZY3 | - |
- |
Haloarcula marismortui DSM 3752 | Q5UZY3 | - |
- |