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@ARTICLE{Cerminara:873619,
      author       = {Cerminara, Michele and Schöne, Antonie and Ritter, Ilona
                      and Gabba, Matteo and Fitter, Jörg},
      title        = {{M}apping {M}ultiple {D}istances in a {M}ultidomain
                      {P}rotein for the {I}dentification of {F}olding
                      {I}ntermediates},
      journal      = {Biophysical journal},
      volume       = {118},
      number       = {3},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-00862},
      pages        = {688-697},
      year         = {2020},
      abstract     = {The investigation and understanding of the folding
                      mechanism of multidomain proteins is still a challenge in
                      structural biology. The use of single-molecule Förster
                      resonance energy transfer offers a unique tool to map
                      conformational changes within the protein structure. Here,
                      we present a study following denaturant-induced unfolding
                      transitions of yeast phosphoglycerate kinase by mapping
                      several inter- and intradomain distances of this two-domain
                      protein, exhibiting a quite heterogeneous behavior. On the
                      one hand, the development of the interdomain distance during
                      the unfolding transition suggests a classical two-state
                      unfolding behavior. On the other hand, the behavior of some
                      intradomain distances indicates the formation of a compact
                      and transient molten globule intermediate state.
                      Furthermore, different intradomain distances measured within
                      the same domain show pronounced differences in their
                      unfolding behavior, underlining the fact that the choice of
                      dye attachment positions within the polypeptide chain has a
                      substantial impact on which unfolding properties are
                      observed by single-molecule Förster resonance energy
                      transfer measurements. Our results suggest that, to fully
                      characterize the complex folding and unfolding mechanism of
                      multidomain proteins, it is necessary to monitor multiple
                      intra- and interdomain distances because a single reporter
                      can lead to a misleading, partial, or oversimplified
                      interpretation.},
      cin          = {ICS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-5-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31916943},
      UT           = {WOS:000511291400016},
      doi          = {10.1016/j.bpj.2019.12.006},
      url          = {https://juser.fz-juelich.de/record/873619},
}