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@ARTICLE{Grigoriev:901807,
      author       = {Grigoriev, S. V. and Iashina, E. G. and Wu, Baohu and
                      Pipich, V. and Lang, Ch. and Radulescu, Aurel and
                      Bairamukov, V. Yu. and Filatov, M. V. and Pantina, R. A. and
                      Varfolomeeva, E. Yu.},
      title        = {{O}bservation of nucleic acid and protein correlation in
                      chromatin of {H}e{L}a nuclei using small-angle neutron
                      scattering with {D} 2 {O} − {H} 2 {O} contrast variation},
      journal      = {Physical review / E},
      volume       = {104},
      number       = {4},
      issn         = {2470-0053},
      address      = {Woodbury, NY},
      publisher    = {Inst.},
      reportid     = {FZJ-2021-03831},
      pages        = {044404},
      year         = {2021},
      abstract     = {The small-angle neutron scattering (SANS) on HeLa nuclei
                      demonstrates the bifractal nature of the chromatin
                      structural organization. The border line between two fractal
                      structures is detected as a crossover point at
                      Qc≈4×10−2nm−1 in the momentum transfer dependence
                      Q−D. The use of contrast variation (D2O−H2O) in SANS
                      measurements reveals clear similarity in the large scale
                      structural organizations of nucleic acids (NA) and proteins.
                      Both NA and protein structures have a mass fractal
                      arrangement with the fractal dimension of D≈2.5 at scales
                      smaller than 150 nm down to 20 nm. Both NA and proteins show
                      a logarithmic fractal behavior with D≈3 at scales larger
                      than 150 nm up to 6000 nm. The combined analysis of the SANS
                      and atomic force microscopy data allows one to conclude that
                      chromatin and its constitutes (DNA and proteins) are
                      characterized as soft, densely packed, logarithmic fractals
                      on the large scale and as rigid, loosely packed, mass
                      fractals on the smaller scale. The comparison of the partial
                      cross sections from NA and proteins with one from chromatin
                      as a whole demonstrates spatial correlation of two
                      chromatin's components in the range up to 900 nm. Thus
                      chromatin in HeLa nuclei is built as the unified structure
                      of the NA and proteins entwined through each other.
                      Correlation between two components is lost upon scale
                      increases toward 6000 nm. The structural features at the
                      large scale, probably, provide nuclei with the flexibility
                      and chromatin-free space to build supercorrelations on the
                      distance of 103 nm resembling cycle cell activity, such as
                      an appearance of nucleoli and a DNA replication.},
      cin          = {JCNS-FRM-II / JCNS-1 / JCNS-4 / MLZ},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-4-20201012 /
                      I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34781557},
      UT           = {WOS:000706513200004},
      doi          = {10.1103/PhysRevE.104.044404},
      url          = {https://juser.fz-juelich.de/record/901807},
}