1. High α-helical content (73%) in SS-8 correlates with strong antifreeze activity, while structural disruption abolishes activity.
2. Blocked N-terminal methionine in SS-8 is crucial for activity, as its removal reduces antifreeze activity despite minimal helical content change.
AFP011004
General Information
| Protein Name | Ice-structuring protein SS-8 |
| UniProt ID | P04368 |
| Species | Myoxocephalus scorpius (Shorthorn sculpin) (Cottus scorpius) |
| Sequence Length | 45 |
| Sequence | |
| Structure | AFDB ID: AF-P04368-F1-model_v4 |
| Solvent Accessible Surface Area | Total SASA | 2856.64 Ų | Polar SASA | 1076.72 Ų | Apolar SASA | 3933.36 Ų |
AFP011004000
| Mutation | Wild Type |
| Sequence |
Thermal Hysteresis
| PMID | 4029130 |
| DOI | 10.1111/j.1432-1033.1985.tb09081.x |
| Protein Name | shorthorn sculpin AFP SS-8 |
| Thermal Hysteresis | Tab.2 Properties of sculpin and flounder AFP, and the cleavage peptides of sculpin AFP. |
Brief description
|
PMID: 4029130
DOI: 10.1111/j.1432-1033.1985.tb09081.x |
AFP011004001
| Mutation | 1del |
| Sequence |
Thermal Hysteresis
| PMID | 4029130 |
| DOI | 10.1111/j.1432-1033.1985.tb09081.x |
| Protein Name | shorthorn sculpin AFP CNBr SS-8 |
| Thermal Hysteresis | Tab.2 Properties of sculpin and flounder AFP, and the cleavage peptides of sculpin AFP. |
Brief description
|
PMID: 4029130
DOI: 10.1111/j.1432-1033.1985.tb09081.x |
1. High α-helical content (73%) in SS-8 correlates with strong antifreeze activity, while structural disruption abolishes activity.
2. Blocked N-terminal methionine in SS-8 is crucial for activity, as its removal reduces antifreeze activity despite minimal helical content change. |