Difference between revisions of "Part:BBa K3498009"
(Ranaspumin-2 Coding Protein) |
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Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the túngara frog (Engystomops pustulosus). This has been confirmed by experiments showing that recombinant Rsn-2 provides a significant reduction in the surface tension of aqueous solutions at concentrations as low as 10 μg mL−1 (Mackenzie et al., 2009). | Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the túngara frog (Engystomops pustulosus). This has been confirmed by experiments showing that recombinant Rsn-2 provides a significant reduction in the surface tension of aqueous solutions at concentrations as low as 10 μg mL−1 (Mackenzie et al., 2009). | ||
Rsn-2 has no sequence similarity to hydrophobins, lipopeptides, or lung surfactants, involves no associated lipid, and is active at much lower concentrations than are normally required for foaming of denatured proteins. Consequently, it represents a new class of surfactant protein (Mackenzie et al., 2009). | Rsn-2 has no sequence similarity to hydrophobins, lipopeptides, or lung surfactants, involves no associated lipid, and is active at much lower concentrations than are normally required for foaming of denatured proteins. Consequently, it represents a new class of surfactant protein (Mackenzie et al., 2009). | ||
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| + | <span class='h3bb'>Sequence and Features</span> | ||
| + | <partinfo>BBa_K3498009 SequenceAndFeatures</partinfo> | ||
Latest revision as of 05:46, 22 September 2020
Ranaspumin-2 protein
Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the túngara frog (Engystomops pustulosus). This has been confirmed by experiments showing that recombinant Rsn-2 provides a significant reduction in the surface tension of aqueous solutions at concentrations as low as 10 μg mL−1 (Mackenzie et al., 2009). Rsn-2 has no sequence similarity to hydrophobins, lipopeptides, or lung surfactants, involves no associated lipid, and is active at much lower concentrations than are normally required for foaming of denatured proteins. Consequently, it represents a new class of surfactant protein (Mackenzie et al., 2009).
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]