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@ARTICLE{Stanyon:172110,
      author       = {Stanyon, Helen F. and Cong, Xiaojing and Chen, Yan and
                      Shahidullah, Nabeela and Rossetti, Giulia and Dreyer, Jens
                      and Papamokos, George and Carloni, Paolo and Viles, John H.},
      title        = {{D}eveloping predictive rules for coordination geometry
                      from visible circular dichroism of {C}opper({II}) and
                      {N}ickel({II}) ions in histidine and amide main-chain
                      complexes},
      journal      = {The FEBS journal},
      volume       = {281},
      number       = {17},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2014-05653},
      pages        = {3945 - 3954},
      year         = {2014},
      abstract     = {Circular Dichroism (CD) spectroscopy in the visible region
                      (Vis-CD) is a powerful technique to study metal-protein
                      interactions. It can resolve individual d–d electronic
                      transitions as separate bands and is particularly sensitive
                      to the chiral environment of the transition metals. Modern
                      quantum chemical methods enable CD spectra calculations from
                      which, along with direct comparison with the experimental CD
                      data, the conformations and the stereochemistry of the
                      metal-protein complexes can be assigned. However, a clear
                      understanding of the observed spectra and the molecular
                      configuration is largely lacking. In this study, we compare
                      the experimental and computed Vis-CD spectra of Cu2+-loaded
                      model peptides in square-planar complexes. We find that the
                      spectra can readily discriminate the coordination pattern of
                      Cu2+ bound exclusively to main-chain amides from that
                      involving both main-chain amides and a side-chain (i.e.
                      histidine side chain). Based on the results, we develop a
                      set of empirical rules that relates the appearance of
                      particular Vis-CD spectral features to the conformation of
                      the complex. These rules can be used to gain insight into
                      coordination geometries of other Cu2+ or Ni2+-protein
                      complexes.},
      cin          = {IAS-5 / INM-9 / GRS / JSC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-588b)1026307295 / I:(DE-Juel1)JSC-20090406},
      pnm          = {411 - Computational Science and Mathematical Methods
                      (POF2-411)},
      pid          = {G:(DE-HGF)POF2-411},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000341721000014},
      pubmed       = {pmid:25039600},
      doi          = {10.1111/febs.12934},
      url          = {https://juser.fz-juelich.de/record/172110},
}