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@ARTICLE{Bustorff:1019402,
      author       = {Bustorff, Nuno and Fitter, Jörg},
      title        = {{F}eatures of {P}rotein {U}nfolding {T}ransitions and
                      {T}heir {R}elation to {D}omain {T}opology {P}robed by
                      {S}ingle-{M}olecule {FRET}},
      journal      = {Biomolecules},
      volume       = {13},
      number       = {9},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2023-05362},
      pages        = {1280 -},
      year         = {2023},
      abstract     = {A protein fold is defined as a structural arrangement of a
                      secondary structure in a threedimensionalspace. It would be
                      interesting to know whether a particular fold can be
                      assigned to certainfeatures of the corresponding
                      folding/unfolding transitions. To understand the underlying
                      principlesof the manifold folding transitions in more
                      detail, single-molecule FRET is the method of choice.Taking
                      the two-domain protein phosphoglycerate kinase (PGK) as an
                      example, we investigateddenaturant-induced unfolded states
                      of PGK using the above method. For this purpose,
                      differentintramolecular distances within the two domains
                      were measured. In addition to the known two-statetransition,
                      a transition with a compact folding intermediate was also
                      identified in each of the twodomains. Based on the
                      structural homology of the domains (characterized by a
                      Rossmann fold)and the striking similarity in the features of
                      the measured distance changes during unfolding,
                      clearevidence emerged that the underlying domain topology
                      plays an important role in determining theobserved
                      structural changes.},
      cin          = {IBI-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-6-20200312},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535)},
      pid          = {G:(DE-HGF)POF4-5352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37759680},
      UT           = {WOS:001074347000001},
      doi          = {10.3390/biom13091280},
      url          = {https://juser.fz-juelich.de/record/1019402},
}