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@ARTICLE{Balacescu:872562,
      author       = {Balacescu, Livia and Schrader, Tobias E. and Radulescu,
                      Aurel and Zolnierczuk, Piotr and Holderer, Olaf and Pasini,
                      Stefano and Fitter, Jörg and Stadler, Andreas M.},
      title        = {{T}ransition between protein-like and polymer-like dynamic
                      behavior: {I}nternal friction in unfolded apomyoglobin
                      depends on denaturing conditions},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-00068},
      pages        = {1570},
      year         = {2020},
      abstract     = {Equilibrium dynamics of different folding intermediates and
                      denatured states is strongly connected to the exploration of
                      the conformational space on the nanosecond time scale and
                      might have implications in understanding protein folding.
                      For the first time, the same protein system apomyoglobin has
                      been investigated using neutron spin-echo spectroscopy in
                      different states: native-like, partially folded (molten
                      globule) and completely unfolded, following two different
                      unfolding paths: using acid or guanidinium chloride (GdmCl).
                      While the internal dynamics of the native-like state can be
                      understood using normal mode analysis based on high
                      resolution structural information of myoglobin, for the
                      unfolded and even for the molten globule states, models from
                      polymer science are employed. The Zimm model accurately
                      describes the slowly-relaxing, expanded GdmCl-denaturated
                      state, ignoring the individuality of the different aminoacid
                      side chain. The dynamics of the acid unfolded and molten
                      globule state are similar in the framework of the Zimm model
                      with internal friction, where the chains still interact and
                      hinder each other: the first Zimm relaxation time is as
                      large as the internal friction time. Transient formation of
                      secondary structure elements in the acid unfolded and
                      presence of α-helices in the molten globule state lead to
                      internal friction to a similar extent.},
      cin          = {JCNS-FRM-II / ICS-5 / JCNS-1 / JCNS-SNS},
      ddc          = {600},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-SNS-20110128},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)J-NSE-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32005832},
      UT           = {WOS:000562877200006},
      doi          = {10.1038/s41598-020-57775-4},
      url          = {https://juser.fz-juelich.de/record/872562},
}