AI Article Synopsis
- The study focuses on incorporating a highly asymmetric F0F1 ATP synthase complex from Micrococcus luteus into polymer membranes, showing its effective integration using weak surfactants without damaging the protein.
- Techniques like dynamic light scattering and cryo electron microscopy confirm that this method allows for a uniform distribution of proteins on polymer surfaces, unlike what happens on glass.
- By utilizing antibodies and topographic profiling, researchers can identify the orientation of ATP synthase, paving the way for enhanced quantification of protein functions in model systems that mimic biological environments.
Article Abstract
We report the vectorial incorporation of a highly asymmetric F0F1 ATP synthase complex from Micrococcus luteus into polymer-supported membranes. Dynamic light scattering and cryo electron microscopy confirm that the use of weak surfactants (bile acid) allows for the non-disruptive protein incorporation into lipid vesicles. Spreading of vesicles with ATP synthase onto a cellulose support results in a homogeneous distribution of proteins, in contrast to a patchy image observed on bare glass slides. The orientation of ATP synthase can be identified using an antibody to the ATP binding site as well as from topographic profiles of the surface. The method to "align" transmembrane proteins in supported membranes would open a possibility to quantify protein functions in biomimetic model systems.
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| http://dx.doi.org/10.1002/mabi.200800128 | DOI Listing |
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