% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Gonalves:201313,
      author       = {Gonçalves, Marcos Brown and Dreyer, Jens and Lupieri,
                      Paola and Barrera-Patiño, Claudia and Ippoliti, Emiliano
                      and Webb, Martin R. and Corrie, John E. T. and Carloni,
                      Paolo},
      title        = {{S}tructural prediction of a rhodamine-based biosensor and
                      comparison with biophysical data},
      journal      = {Physical chemistry, chemical physics},
      volume       = {15},
      number       = {6},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2015-03618},
      pages        = {2177 - 2183},
      year         = {2013},
      abstract     = {The predicted structure has been calculated for a
                      protein-based biosensor for inorganic phosphate (Pi),
                      previously developed by some of us (Okoh et al.,
                      Biochemistry, 2006, 45, 14764). This is the phosphate
                      binding protein from Escherichia coli labelled with two
                      rhodamine fluorophores. Classical molecular dynamics and
                      hybrid Car–Parrinello/molecular mechanics simulations
                      allow us to provide molecular models of the biosensor both
                      in the presence and in the absence of Pi. In the latter
                      case, the rhodamine fluorophores maintain a stacked
                      conformation in a ‘face A to face B’ orientation, which
                      is different from the ‘face A to face A’ stacked
                      orientation of free fluorophores in aqueous solution (Ilich
                      et al., Spectrochim. Acta, Part A, 1996, 52, 1323). A
                      protein conformation change upon binding Pi prevents
                      significant stacking of the two rhodamines. In both states,
                      the rhodamine fluorophores form hydrophobic contact with
                      LEU291, without establishing significant hydrogen bonds with
                      the protein. The accuracy of the models is established by a
                      comparison between calculated and experimentalabsorption and
                      circular dichroism spectra.},
      cin          = {GRS / IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000313566300050},
      pubmed       = {pmid:23247608},
      doi          = {10.1039/C2CP42396K},
      url          = {https://juser.fz-juelich.de/record/201313},
}