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

在CRC 1035中，我们的目标是使用先进的荧光方法来研究生物分子的构象动力学。我们已经开发了3c FRET，这样我们就可以检测单个生物分子的协调运动。在接下来的四年中，我们将研究热休克蛋白70 s内的变构效应，即热休克蛋白70和热休克蛋白90之间的客户转移（与Buchner/Sattler，A03），剪接体的动力学（与Sattler，B 03），GroEL和GroES对蛋白质折叠的影响以及活细胞中分子伴侣和核糖体之间的相互作用（与Hayer-Hartl/Hartl，A12），以及基于肽的淀粉样蛋白抑制剂和小热休克蛋白（与Kapurniotu，B 06; Reif，B 07）和HBx（与Schütz，B15）的动力学。

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).