@article{SchubertSchulzeProdromouetal.2021,
  author    = {Schubert, Jonathan and Schulze, Andrea and Prodromou, Chrisostomos and Neuweiler, Hannes},
  title     = {Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics},
  series = {Nature Communications},
  volume    = {12},
  journal   = {Nature Communications},
  doi       = {10.1038/s41467-021-27286-5},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-265754},
  year      = {2021},
  abstract  = {Many proteins are molecular machines, whose function is dependent on multiple conformational changes that are initiated and tightly controlled through biochemical stimuli. Their mechanistic understanding calls for spectroscopy that can probe simultaneously such structural coordinates. Here we present two-colour fluorescence microscopy in combination with photoinduced electron transfer (PET) probes as a method that simultaneously detects two structural coordinates in single protein molecules, one colour per coordinate. This contrasts with the commonly applied resonance energy transfer (FRET) technique that requires two colours per coordinate. We demonstrate the technique by directly and simultaneously observing three critical structural changes within the Hsp90 molecular chaperone machinery. Our results reveal synchronicity of conformational motions at remote sites during ATPase-driven closure of the Hsp90 molecular clamp, providing evidence for a cooperativity mechanism in the chaperone's catalytic cycle. Single-molecule PET fluorescence microscopy opens up avenues in the multi-dimensional exploration of protein dynamics and allosteric mechanisms.},
  language  = {en}
}
@article{HartelGloggerJonesetal.2016,
  author    = {Hartel, Andreas J.W. and Glogger, Marius and Jones, Nicola G. and Abuillan, Wasim and Batram, Christopher and Hermann, Anne and Fenz, Susanne F. and Tanaka, Motomu and Engstler, Markus},
  title     = {N-glycosylation enables high lateral mobility of GPI-anchored proteins at a molecular crowding threshold},
  series = {Nature Communications},
  volume    = {7},
  journal   = {Nature Communications},
  doi       = {10.1038/ncomms12870},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-171368},
  year      = {2016},
  abstract  = {The protein density in biological membranes can be extraordinarily high, but the impact of molecular crowding on the diffusion of membrane proteins has not been studied systematically in a natural system. The diversity of the membrane proteome of most cells may preclude systematic studies. African trypanosomes, however, feature a uniform surface coat that is dominated by a single type of variant surface glycoprotein (VSG). Here we study the density-dependence of the diffusion of different glycosylphosphatidylinositol-anchored VSG-types on living cells and in artificial membranes. Our results suggest that a specific molecular crowding threshold (MCT) limits diffusion and hence affects protein function. Obstacles in the form of heterologous proteins compromise the diffusion coefficient and the MCT. The trypanosome VSG-coat operates very close to its MCT. Importantly, our experiments show that N-linked glycans act as molecular insulators that reduce retarding intermolecular interactions allowing membrane proteins to function correctly even when densely packed.},
  language  = {en}
}