1. It was shown that sssAFP-2 mRNA is expressed in various tissues such as skin, dorsal fin, brain, and gill filament, but not in the liver, and exhibits significant seasonal variation.
2. The recombinant protein His-sssAFP-2 was constructed and purified. It has an α-helical structure with a helix content of approximately 74% at 0 ℃. Its thermal hysteresis activity is concentration-dependent. Compared with the winter flounder liver-type antifreeze protein wflAFP-6, it has similar activity on a molar basis but lower activity on a mg/ml basis.
AFP011006
General Information
| Protein Name | Skin-type antifreeze polypeptide AFP-2 |
| UniProt ID | Q9DF23 |
| Nucleotide Sequence ID in NCBI | AF305502 |
| Protein Sequence ID in NCBI | AAG25982.1 |
| Species | Myoxocephalus scorpius (Shorthorn sculpin) (Cottus scorpius) |
| Sequence Length | 92 |
| Sequence | |
| Structure | AF2 predicted Structure: AFP011006 |
| Solvent Accessible Surface Area | Total SASA | 5003.94 Ų | Polar SASA | 1736.02 Ų | Apolar SASA | 6739.96 Ų |
AFP011006000
| Mutation | Wild Type |
| Sequence |
Ice crystal morphology
| PMID | 9722537 |
| DOI | 10.1074/jbc.273.36.23098 |
| Protein Name | shorthorn sculpin AFP sssAFP2 |
| Tag | Hexahistidine |
| Ice crystal morphology | Fig.5 His-sssAFP-2 is an active antifreeze peptide. A and B, shown is ice crystal morphology in the presence of His-sssAFP-2. A, 0.09 mM His-sssAFP-2; B, 1.12 mM His-sssAFP-2. |
Thermal Hysteresis
| PMID | 9722537 |
| DOI | 10.1074/jbc.273.36.23098 |
| Protein Name | shorthorn sculpin AFP sssAFP2 |
| Tag | Hexahistidine |
| Thermal Hysteresis | Fig.5 His-sssAFP-2 is an active antifreeze peptide. C and D, thermal hysteretic activity of His-sssAFP-2 (▲) and wflAFP-6 (■), measured in molar concentration (C) and in mg/ml (D). |
Ice Binding Sites
| PMID | 9722537 |
| DOI | 10.1074/jbc.273.36.23098 |
| Protein Name | shorthorn sculpin AFP sssAFP2 |
| Tag | Hexahistidine |
| IBS | It is proposed that polar residues in the 11-residue repeats (such as Pr in the Pr-X2-Pr-X7 repeats) may interact with the ice-crystal lattice through hydrogen bonding. |
Brief description
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PMID: 9722537
DOI: 10.1074/jbc.273.36.23098 |