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AKB: Biologische Physik

AKB 100: Poster Session I

AKB 100.49: Poster

Samstag, 5. März 2005, 16:45–18:45, Poster TU D

Protein conformation probed by fluorescence — •thomas gensch, thomas dertinger, thomas sorkalla, andreas helten, karl-wilhelm koch, ingo gregor, and joerg enderlein — IBI1, Research Centre Juelich

We study the protein-protein interaction of membrane proteins (ion channels, enzymes) with regulating proteins and activating cofactors by fluorescence spectroscopy methods (time-resolved fluorescence spectroscopy, single molecule spectroscopy, Förster resonance energy transfer). The proteins are made fluorescent in the visible spectral region by two methods: 1. production of fusion proteins of the protein of interest with an autofluorescent protein (like the green fluorescent protein). 2. Specific labelling of single Cysteins with organic fluorophores functionalised with a maleimide group. The properties of two regulating, Ca2+-binding proteins (Calmodulin, GCAP) labelled with different fluorophores have been investigated in detail. Different protein conformations have been identified by different fluorescence properties of the fluorophores. Their Ca2+ dependence is investigated as well as the influence of binding events. First results from model FRET experiments will be presented.