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@ARTICLE{Gupta:824977,
      author       = {Gupta, Sudipta and Biehl, Ralf and Sill, Clemens and
                      Allgaier, J. and Sharp, Melissa and Ohl, Michael and
                      Richter, Dieter},
      title        = {{P}rotein {E}ntrapment in {P}olymeric {M}esh: {D}iffusion
                      in {C}rowded {E}nvironment with {F}ast {P}rocess on {S}hort
                      {S}cales},
      journal      = {Macromolecules},
      volume       = {49},
      number       = {5},
      issn         = {1520-5835},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2016-07473},
      pages        = {1941 - 1949},
      year         = {2016},
      abstract     = {The natural environment of proteins is a crowded
                      environment as in cells, extracellular fluids, or during
                      processing. Semidilute polymer solutions have been a source
                      of rich structural and dynamical properties and mimic a
                      crowded environment, but a proper understanding of protein
                      dynamics in the crowded environment is far lagging. Such a
                      study not only realizes protein’s natural environment in a
                      crowded solution in the cell or during processing but also
                      manifests the underlying protein–polymer interaction. By
                      dispersing model globular proteins like α-lactalbumin (La)
                      and hemoglobin (Hb), in aqueous solution of poly(ethylene
                      oxide) (PEO) we mimic a crowded environment and use
                      state-of-the-art neutron spin echo (NSE) and small-angle
                      neutron scattering (SANS) techniques to observe the
                      corresponding protein dynamics in semidilute polymer
                      solution. NSE can access the fast diffusion process (Dfast)
                      prior to the slow diffusion process on long times and length
                      scales (Dγ). The protein dynamics in a crowded environment
                      can be described analogous to the diffusion in a periodic
                      potential. The fast dynamics corresponds to diffusion inside
                      a trap built by the polymer mesh while the slower process is
                      the long time diffusion on macroscopic length scales also
                      observed by other techniques. We observe the onset of
                      fractional diffusion for higher concentrated polymer
                      solutions.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / JCNS-SNS / JCNS-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-SNS-20110128 / I:(DE-Juel1)JCNS-2-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000371851100047},
      doi          = {10.1021/acs.macromol.5b02281},
      url          = {https://juser.fz-juelich.de/record/824977},
}