This thesis addresses the novel
concept of biological recognition based on membrane curvature. Membrane
curvature is at present perceived as an active way to organize
nanoscale centers for membrane traffic in cells. The ability of protein
domains to assemble in macromolecular scaffolds in response to membrane
organization and molecular cues is a prerequisite for maintaining an
effective cell communication and function. We have developed a new
fluorescence based assay to quantify and understand the molecular
mechanism of membrane curvature sensing by amphipathic anchoring motifs
and BAR (Bin, Amphiphysin, Rvs) domains. The new assay is based on
single liposomes allowing in a high-throughput fashion, the detection
of protein binding to a multitude of curvatures. Using this assay we
are able to detect inhomo-geneous and asynchronous activities,
something not possible with existing assays. The results suggest that
Membrane Curvature Sensing by proteins is not dominated by differences
in affinity and thus prompts a re-evaluation of the current model.