% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{DUrzo:201330,
      author       = {D’Urzo, Annalisa and Konijnenberg, Albert and Rossetti,
                      Giulia and Habchi, Johnny and Li, Jinyu and Carloni, Paolo
                      and Sobott, Frank and Longhi, Sonia and Grandori, Rita},
      title        = {{M}olecular {B}asis for {S}tructural {H}eterogeneity of an
                      {I}ntrinsically {D}isordered {P}rotein {B}ound to a
                      {P}artner by {C}ombined {ESI}-{IM}-{MS} and {M}odeling},
      journal      = {Journal of the American Society for Mass Spectrometry},
      volume       = {26},
      number       = {3},
      issn         = {1879-1123},
      address      = {New York [u.a.]},
      publisher    = {Springer},
      reportid     = {FZJ-2015-03627},
      pages        = {472 - 481},
      year         = {2015},
      abstract     = {Intrinsically disordered proteins (IDPs) form biologically
                      active complexes that can retain a high degree of
                      conformational disorder, escaping structural
                      characterization by conventional approaches. An example is
                      offered by the complex between the intrinsically disordered
                      NTAIL domain and the phosphoprotein X domain (PXD) from
                      measles virus (MeV). Here, distinct conformers of the
                      complex are detected by electrospray ionization-mass
                      spectrometry (ESI-MS) and ion mobility (IM) techniques
                      yielding estimates for the solvent-accessible surface area
                      (SASA) in solution and the average collision cross-section
                      (CCS) in the gas phase. Computational modeling of the
                      complex in solution, based on experimental constraints,
                      provides atomic-resolution structural models featuring
                      different levels of compactness. The resulting models
                      indicate high structural heterogeneity. The intermolecular
                      interactions are predominantly hydrophobic, not only in the
                      ordered core of the complex, but also in the dynamic,
                      disordered regions. Electrostatic interactions become
                      involved in the more compact states. This system represents
                      an illustrative example of a hydrophobic complex that could
                      be directly detected in the gas phase by native mass
                      spectrometry. This work represents the first attempt to
                      modeling the entire NTAIL domain bound to PXD at atomic
                      resolution.},
      cin          = {INM-9 / IAS-5 / GRS / JSC},
      ddc          = {530},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)JSC-20090406},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000350106100011},
      pubmed       = {pmid:25510932},
      doi          = {10.1007/s13361-014-1048-z},
      url          = {https://juser.fz-juelich.de/record/201330},
}