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@INPROCEEDINGS{Biehl:1023000,
      author       = {Biehl, Ralf},
      title        = {{D}omain {M}otions: {P}rotein {D}ynamics seen by {N}eutron
                      {S}pinecho {S}pectroscopy},
      reportid     = {FZJ-2024-01589},
      year         = {2024},
      abstract     = {The biological function of proteins is often related to
                      configurational changes and large-scale domain motions,
                      which are induced or suppressed by the binding of a
                      substrate or due to cosolvents. Domain motions can be
                      related to soft hinges, flexible linker regions or -as in
                      the case of intrinsically disordered proteins- be native to
                      proteins without secondary or tertiary structure. These
                      large-scale domain motions in solution cannot be observed by
                      X-ray crystallography or NMR spectroscopy. Small angle
                      scattering (SAS) by X-rays or neutrons in combination with
                      neutron spin echo spectroscopy (NSE) in solution can be used
                      to observe configurational changes and equilibrium dynamics
                      between functional domains on 1-300 nanosecond timescale.I
                      will present examples for different types of motions related
                      to the structure of proteins and bioconjugates. Thermal
                      unfolded Ribonuclease A shows polymer like dynamics despite
                      the 4 disulfide bonds restricting the degrees of freedom.
                      Prior to full unfolding the protein unfolding dynamics is
                      observed. Polyelectrolytes have structural and dynamical
                      similarities with IDP. The domain protein Phosphoglycerate
                      kinase shows a hinge motion between the main domains related
                      to function. PEGylation seems not to influence this domain
                      motion but adds additional internal dynamics in the
                      protein-polymer complex. Antibodies present a strong
                      dynamics due to the short linkers connecting the Fc with the
                      Fab domains. The observed dynamics is related to internal
                      forces, solvent friction and the role of charge screening.},
      organization  = {Antibodies in Solution: a LINXS - NIST
                       Webinar Series, Online (Sweden)},
      subtyp        = {Invited},
      cin          = {JCNS-1 / IBI-8},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)IBI-8-20200312},
      pnm          = {632 - Materials – Quantum, Complex and Functional
                      Materials (POF4-632) / 6G4 - Jülich Centre for Neutron
                      Research (JCNS) (FZJ) (POF4-6G4) / 5251 - Multilevel Brain
                      Organization and Variability (POF4-525) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-632 / G:(DE-HGF)POF4-6G4 /
                      G:(DE-HGF)POF4-5251 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)31},
      url          = {https://juser.fz-juelich.de/record/1023000},
}