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Conformational changes monitored for a hinge-bending protein by single molecule FRET

Conformational dynamics of proteins
In prokaryotic and even more in eukaryotic cells, the predominant fraction of the proteome belongs to the class of multidomain protein. Our existing knowledge about mechanisms and principles of protein folding results mainly from studies on smaller, single-domain proteins. However, large-scale motions of globular domains are often crucial for the activity of multidomain proteins. By employing single-photon counting with sub-nanosecond time resolution, we make use of extensive multi-parameter fluorescence analysis. Major methods that we apply and develop are single-molecule Förster resonance energy transfer (smFRET), fluorescence correlation spectroscopy (FCS), time-resolved anisotropy decay (TRA) and photo-induced electron transfer (PET).

Biophysics (Aachen):
Jörg Fitter

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