Difference between revisions of "Part:BBa K3498009"

(Ranaspumin-2 Coding Protein)
(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).
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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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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).

Revision as of 01:49, 21 September 2020

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).