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@ARTICLE{Gogonea:14185,
      author       = {Gogonea, V. and Wu, Z. and Lee, X. and Pipich, V. and Li,
                      X.-M. and Ioffe, A. and DiDonato, J.A. and Hazen, S.L.},
      title        = {{C}ongruency between biophysical data from multiple
                      platforms and molecular dynamics simulation of the double
                      super helix model of nascent high-density lipoprotein},
      journal      = {Biochemistry},
      volume       = {49},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-14185},
      pages        = {7323 - 7343},
      year         = {2010},
      note         = {This study was supported by National Institutes of Health
                      Grants P01 HL098055, P01 HL076491-055328, P01 HL087018-02001
                      and R01 DK 080732-01.},
      abstract     = {The predicted structure and molecular trajectories from >80
                      ns molecular dynamics simulation of the solvated
                      Double-Super Helix (DSH) model of nascent high-density
                      lipoprotein (HDL) were determined and compared with
                      experimental data on reconstituted nascent HDL obtained from
                      multiple biophysical platforms, including small angle
                      neutron scattering (SANS) with contrast variation,
                      hydrogen-deuterium exchange tandem mass spectrometry
                      (H/D-MS/MS), nuclear magnetic resonance spectroscopy (NMR),
                      cross-linking tandem mass spectrometry (MS/MS), fluorescence
                      resonance energy transfer (FRET), electron spin resonance
                      spectroscopy (ESR), and electron microscopy. In general,
                      biophysical constraints experimentally derived from the
                      multiple platforms agree with the same quantities evaluated
                      using the simulation trajectory. Notably, key structural
                      features postulated for the recent DSH model of nascent HDL
                      are retained during the simulation, including (1) the
                      superhelical conformation of the antiparallel apolipoprotein
                      A1 (apoA1) chains, (2) the lipid micellar-pseudolamellar
                      organization, and (3) the solvent-exposed Solar Flare loops,
                      proposed sites of interaction with LCAT (lecithin
                      cholesteryl acyltransferase). Analysis of salt bridge
                      persistence during simulation provides insights into
                      structural features of apoA1 that forms the backbone of the
                      lipoprotein. The combination of molecular dynamics
                      simulation and experimental data from a broad range of
                      biophysical platforms serves as a powerful approach to
                      studying large macromolecular assemblies such as
                      lipoproteins. This application to nascent HDL validates the
                      DSH model proposed earlier and suggests new structural
                      details of nascent HDL.},
      keywords     = {Apolipoprotein A-I: chemistry / Biophysics / Deuterium /
                      Hydrogen / Lipids / Lipoproteins: chemistry / Lipoproteins,
                      HDL: chemistry / Macromolecular Substances / Magnetic
                      Resonance Spectroscopy / Molecular Dynamics Simulation /
                      Phosphatidylcholine-Sterol O-Acyltransferase / Protein
                      Structure, Secondary / Apolipoprotein A-I (NLM Chemicals) /
                      Lipids (NLM Chemicals) / Lipoproteins (NLM Chemicals) /
                      Lipoproteins, HDL (NLM Chemicals) / Macromolecular
                      Substances (NLM Chemicals) / Hydrogen (NLM Chemicals) /
                      Deuterium (NLM Chemicals) / Phosphatidylcholine-Sterol
                      O-Acyltransferase (NLM Chemicals) / J (WoSType)},
      cin          = {IFF-4 / IFF-5 / Jülich Centre for Neutron Science JCNS
                      (JCNS) ; JCNS},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB784 / I:(DE-Juel1)VDB785 /
                      I:(DE-Juel1)JCNS-20121112},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20687589},
      pmc          = {pmc:PMC2940317},
      UT           = {WOS:000281052600010},
      doi          = {10.1021/bi100588a},
      url          = {https://juser.fz-juelich.de/record/14185},
}