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@ARTICLE{Sebastiani:281720,
      author       = {Sebastiani, F. and Longo, M. and Orecchini, A. and Comez,
                      L. and De Francesco, A. and Muthmann, M. and Teixeira, S. C.
                      M. and Petrillo, C. and Sacchetti, F. and Paciaroni, A.},
      title        = {{H}ydration-dependent dynamics of human telomeric
                      oligonucleotides in the picosecond timescale: {A} neutron
                      scattering study},
      journal      = {The journal of chemical physics},
      volume       = {143},
      number       = {1},
      issn         = {1089-7690},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {FZJ-2016-01408},
      pages        = {015102 -},
      year         = {2015},
      note         = {"final draft post referee" can nicht beigebracht werden},
      abstract     = {The dynamics of the human oligonucleotide AG 3(T2 AG 3)3
                      has been investigated by incoherent neutron scattering in
                      the sub-nanosecond timescale. A hydration-dependent
                      dynamical activation of thermal fluctuations in weakly
                      hydrated samples was found, similar to that of protein
                      powders. The amplitudes of such thermal fluctuations were
                      evaluated in two different exchanged wave-vector ranges, so
                      as to single out the different contributions from intra- and
                      inter-nucleotide dynamics. The activation energy was
                      calculated from the temperature-dependent characteristic
                      times of the corresponding dynamical processes. The trends
                      of both amplitudes and activation energies support a picture
                      where oligonucleotides possess a larger conformational
                      flexibility than long DNA sequences. This additional
                      flexibility, which likely results from a significant
                      relative chain-end contribution to the average chain
                      dynamics, could be related to the strong structural
                      polymorphism of the investigated oligonucleotides.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000357873900039},
      pubmed       = {pmid:26156493},
      doi          = {10.1063/1.4923213},
      url          = {https://juser.fz-juelich.de/record/281720},
}