Single molecule fluorescence methods for investigating conformational dynamics and allosteric effects in chaperones (A11)

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Within the CRC1035, our objective is to use advanced fluorescence methods to investigate the conformational dynamics of biomolecules. We have developed 3c FRET such that we can detect coordinated motions in individual biomolecules. During the next four years, we will investigate allosteric effects within Hsp70s, the transfer of clients between Hsp70 and Hsp90 (with Buchner/Sattler, A03), the dynamics of the spliceosome (with Sattler, B03), the influence of GroEL and GroES on protein folding as well as interactions between chaperones and ribosomes in living cells (with Hayer-Hartl/Hartl, A12), and the dynamics of peptide-based amyloid inhibitors and small heat shock proteins (with Kapurniotu, B06; Reif, B07) and HBx (with Schütz, B15).