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@ARTICLE{Samantray:902426,
      author       = {Samantray, Suman and Olubiyi, Olujide O. and Strodel,
                      Birgit},
      title        = {{T}he {I}nfluences of {S}ulphation, {S}alt {T}ype, and
                      {S}alt {C}oncentration on the {S}tructural {H}eterogeneity
                      of {G}lycosaminoglycans},
      journal      = {International journal of molecular sciences},
      volume       = {22},
      number       = {21},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2021-04248},
      pages        = {11529 -},
      year         = {2021},
      abstract     = {The increasing recognition of the biochemical importance of
                      glycosaminoglycans (GAGs) has in recent times made them the
                      center of attention of recent research investigations. It
                      became evident that subtle conformational factors play an
                      important role in determining the relationship between the
                      chemical composition of GAGs and their activity. Therefore,
                      a thorough understanding of their structural flexibility is
                      needed, which is addressed in this work by means of all-atom
                      molecular dynamics (MD) simulations. Four major GAGs with
                      different substitution patterns, namely hyaluronic acid as
                      unsulphated GAG, heparan-6-sulphate, chondroitin-4-sulphate,
                      and chondroitin-6-sulphate, were investigated to elucidate
                      the influence of sulphation on the dynamical features of
                      GAGs. Moreover, the effects of increasing NaCl and KCl
                      concentrations were studied as well. Different structural
                      parameters were determined from the MD simulations, in
                      combination with a presentation of the free energy landscape
                      of the GAG conformations, which allowed us to unravel the
                      conformational fingerprints unique to each GAG. The largest
                      effects on the GAG structures were found for sulphation at
                      position 6, as well as binding of the metal ions in the
                      absence of chloride ions to the carboxylate and sulphate
                      groups, which both increase the GAG conformational
                      flexibility.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / 5241 - Molecular Information Processing in
                      Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34768961},
      UT           = {WOS:000719525400001},
      doi          = {10.3390/ijms222111529},
      url          = {https://juser.fz-juelich.de/record/902426},
}