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@ARTICLE{Rossetti:201098,
      author       = {Rossetti, Giulia},
      title        = {{L}igand {B}inding on {I}ntrinsic {D}isordered {P}roteins:
                      {F}ocus on {H}uman {A}lpha-{S}ynuclein},
      journal      = {Biophysical journal},
      volume       = {104},
      number       = {2},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {FZJ-2015-03403},
      pages        = {379a},
      year         = {2013},
      abstract     = {Intrinsically disordered proteins (IDPs) are involved in a
                      wide variety of human diseases (1). Hence, interfering with
                      the function of IDP-disease-associated proteins offers a
                      highly attractive objective for drug development (2).
                      Unfortunately, rational approaches have been hampered so far
                      because of variety of problems absent in traditional drug
                      design protocols. These issues include the highly dynamic
                      nature of IDPs (3), the presence of local and long-range
                      conformational rearrangements (4), transient secondary
                      structure, transient long-range tertiary structure (5,
                      6).Here we present a combined NMR/molecular dynamics
                      protocol that provides quantitative information on ligand
                      poses to IDPs. The approach is based on a geometrical-based
                      analysis of MD trajectory with a flexibility index able to
                      detect conformational transition of residues' backbone
                      (Caliandro, C, Rossetti, G, Carloni, P, 2012 JCTC in press).
                      The protocol is applied on dopamine in complex with the
                      naturally unfolded protein human α-synuclein. The proposed
                      protocol is very general and it could be used to investigate
                      the pose of novel molecules binding to any IDP.},
      cin          = {JSC / IAS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {411 - Computational Science and Mathematical Methods
                      (POF2-411)},
      pid          = {G:(DE-HGF)POF2-411},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000316074303437},
      doi          = {10.1016/j.bpj.2012.11.2111},
      url          = {https://juser.fz-juelich.de/record/201098},
}