Berlin 2012 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 7: Posters: Proteins
BP 7.16: Poster
Montag, 26. März 2012, 17:30–19:30, Poster A
Characterization of novel bimolecular fluorescence complementation (BiFC) protein complexes by single-molecule spectroscopy — •Sven zur Oven-Krockhaus1, Sebastien Peter1, Alfred Meixner2, Klaus Harter1, and Frank Schleifenbaum1 — 1Zentrum für Molekularbiologie der Pflanzen, Tübingen, Deutschland — 2Institut für physikalische und theoretische Chemie, Tübingen, Deutschland
The identification and characterization of protein-protein interaction networks in living organisms is of major importance in current proteome sciences. Bimolecular fluorescence complementation (BiFC) constitutes an innovative method to visualize interaction partners in living cells. As this technique utilizes molecular markers, a competent knowledge of their photophysical properties is essential. In the case of multicolor BiFC, two nearby fragments of different GFP mutants can spontaneously recombine to a functional fluorescent protein complex. Even though they only differ in few amino acids, differently composed complexes show a significant diversity in their spectroscopic properties. As many photophysical features are concealed in bulk measurements, a single molecule approach has been employed to characterize model systems of these BiFC complexes. Several hundred single molecule spectra and fluorescence intensity time traces were accumulated in order to identify the spectroscopically most relevant amino acids in the protein shell structure - uniquely revealing their influence on the shells' mechanical flexibility.