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Interaction of recombinant ankyrin-binding domain (ankBDn) and its mutants with PE/PC lipid monolayer.

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posted on 2011-06-28, 00:20 authored by Marcin Wolny, Michał Grzybek, Ewa Bok, Anna Chorzalska, Marc Lenoir, Aleksander Czogalla, Klaudia Adamczyk, Adam Kolondra, Witold Diakowski, Michael Overduin, Aleksander F. Sikorski

A) Interaction of ankBDn and its mutants with PE/PC 3∶2 (w/w) monolayer. The first 38 amino acid residues of ankBDn are shown; substitutions are marked in red. The ankBDn plateau level is defined as 100% PE/PC binding activity and is equal to ∼2.5 mN/m. Plateau levels were obtained at a protein concentration of ∼25–35 nM. Higher plateau levels indicate increased penetration of the lipid monolayer by protein. Average values were calculated from at least three measurements. Significant differences from the plateau value obtained for wild-type ankBDn are marked (Student's t test): * p<0.05; ** p<0.0001. Details in “Materials and Methods”. B) Interaction of ankBDn and its quadruple mutant SSSA with PS/PC 3∶2 (w/w) monolayer. Interaction of ankBDn with PE/PC monolayer was defined as 100%.

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