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@ARTICLE{PalominoHernandez:996739,
      author       = {Palomino-Hernandez, Oscar and Santambrogio, Carlo and
                      Rossetti, Giulia and Fernandez, Claudio O. and Grandori,
                      Rita and Carloni, Paolo},
      title        = {{M}olecular {D}ynamics-{A}ssisted {I}nterpretation of
                      {E}xperimentally {D}etermined {I}ntrinsically {D}isordered
                      {P}rotein {C}onformational {C}omponents: {T}he {C}ase of
                      {H}uman α-{S}ynuclein},
      journal      = {The journal of physical chemistry / B},
      volume       = {126},
      number       = {20},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2023-01155},
      pages        = {3632 - 3639},
      year         = {2022},
      abstract     = {Mass spectrometry and single molecule force microscopy are
                      two experimental approaches able to provide structural
                      information on intrinsically disordered proteins (IDPs).
                      These techniques allow the dissection of conformational
                      ensembles in their main components, although at a
                      low-resolution level. In this work, we interpret the results
                      emerging from these experimental approaches on human alpha
                      synuclein (AS) by analyzing a previously published 73
                      μs-long molecular-dynamics (MD) simulation of the protein
                      in explicit solvent. We further compare MD-based predictions
                      of single molecule Förster resonance energy transfer
                      (smFRET) data of AS in solution with experimental data. The
                      combined theoretical and experimental data provide a
                      description of AS main conformational ensemble, shedding
                      light into its intramolecular interactions and overall
                      structural compactness. This analysis could be easily
                      transferred to other IDPs.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 5111 - Domain-Specific Simulation $\&$ Data
                      Life Cycle Labs (SDLs) and Research Groups (POF4-511)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-5111},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35543707},
      UT           = {WOS:000806447100002},
      doi          = {10.1021/acs.jpcb.1c10954},
      url          = {https://juser.fz-juelich.de/record/996739},
}