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@ARTICLE{Rosenkranz:4647,
      author       = {Rosenkranz, T. and Katranidis, A. and Atta, D. and
                      Enderlein, J. and Gregor, I. and Grzelakowski, M. and
                      Rigler, P. and Meier, W. and Fitter, J.},
      title        = {{O}bserving {P}roteins as {S}ingle {M}olecules
                      {E}ncapsulated in {S}urface-{T}ethered {P}olymeric
                      {N}anocontainers},
      journal      = {ChemBioChem},
      volume       = {10},
      issn         = {1439-4227},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {PreJuSER-4647},
      pages        = {702 - 709},
      year         = {2009},
      note         = {Jurgen Groll (SusTech GmbH $\&$ Co KG, Darmstadt) is
                      greatly acknowledged for providing us with a protocol for
                      cover slide coatings. We thank Iris v. d. Hocht for
                      providing Atto655-labeled DOPE. T.R. acknowledges financial
                      support by the International Helmholtz Research School on
                      Biophysics and Soft Matter ("Bio-Soft'). J.F thanks G. Buldt
                      (Forschungszentrum Julich) for continuous and sustainable
                      support in his institute.},
      abstract     = {Immobilizing biomolecules provides the advantage of
                      observing them individually for extended time periods, which
                      is impossible to accomplish for freely diffusing molecules
                      in solution. In order to immobilize individual protein
                      molecules, we encapsulated them in polymeric vesicles made
                      of amphiphilic triblock copolymers and tethered the vesicles
                      to a cover slide surface. A major goal of this study is to
                      investigate polymeric vesicles with respect to their
                      suitability for protein-folding studies. The fact that
                      polymeric vesicles possess an extreme stability under
                      various chemical conditions is supported by our observation
                      that harsh unfolding conditions do not perturb the
                      structural integrity of the vesicles. Moreover,
                      polymerosomes prove to be permeable to GdnHCl and, thereby,
                      ideally suited for unfolding and refolding studies with
                      encapsulated proteins. We demonstrate this with encapsulated
                      phosphoglycerate kinase, which was fluorescently labeled
                      with Atto655, a dye that exhibits pronounced photoinduced
                      electron transfer (PET) to a nearby tryptophan residue in
                      the native state. Under unfolding conditions, PET was
                      reduced, and we monitored alternating unfolding and
                      refolding conditions for individual encapsulated proteins.},
      keywords     = {Fluorescent Dyes: metabolism / Fungal Proteins: chemistry /
                      Fungal Proteins: metabolism / Hydrophobic and Hydrophilic
                      Interactions / Immobilized Proteins: chemistry / Immobilized
                      Proteins: metabolism / Liposomes: chemistry / Nanoparticles:
                      chemistry / Photochemical Processes / Polymers: chemistry /
                      Protein Denaturation / Protein Folding / Protein
                      Renaturation / Saccharomyces cerevisiae / Surface Properties
                      / Fluorescent Dyes (NLM Chemicals) / Fungal Proteins (NLM
                      Chemicals) / Immobilized Proteins (NLM Chemicals) /
                      Liposomes (NLM Chemicals) / Polymers (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Chemistry, Medicinal},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19191249},
      UT           = {WOS:000264168000015},
      doi          = {10.1002/cbic.200800739},
      url          = {https://juser.fz-juelich.de/record/4647},
}