On the structural dynamics of multi-domain proteins
The molecular chaperone Heat shock protein Hsp90 is one of the most abundant proteins in eukaryotic cells. Its function is related to a characteristic interconversion between an open and closed conformational state. Single-molecule FRET (smFRET) studies and MD simulations show that its dynamics are correlated over a large timescale ranging from local dynamics of ns to large conformational changes on the sec timescale. However, the underlying mechanism of the interconversion between the two states and the correlation over the timescales is still unclear. On the example of the Hsp90 system we wish to establish a comprehensive dynamical picture across timescales by using high-resolution neutron spectroscopy and smFRET data. This would in addition be an important step towards integrative modelling approaches. Finally, we also propose to investigate how the internal dynamics of proteins is impacted by fluorescent labelling, which is crucial for smFRET studies. This research is part of the PhD projects of Christian Beck and Benedikt Sohmen.
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SOHMEN Benedikt; BECK Christian; GRIMALDO Marco; HOFFMANN Ingo; HUGEL Thorsten; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo; THURN Johann and VORREITER Jolanta. (2018). On the structural dynamics of multi-domain proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-838
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