% 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{HaberPohlmeier:56497,
      author       = {Haber-Pohlmeier, S. and Abarca Heidemann, K. and Körschen,
                      H. G. and Kaur Dhiman, H. and Heberle, J. and Schwalbe, H.
                      and Klein-Seetharaman, J. and Kaupp, U. B. and Pohlmeier,
                      A.},
      title        = {{B}inding of {C}a2+ to glutamic acid-rich polypeptides from
                      the rod outer segment},
      journal      = {Biophysical journal},
      volume       = {92},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-56497},
      pages        = {3207 - 3214},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Rod photoreceptors contain three different glutamic
                      acid-rich proteins (GARPs) that have been proposed to
                      control the propagation of Ca(2+) from the site of its entry
                      at the cyclic nucleotide-gated channel to the cytosol of the
                      outer segment. We tested this hypothesis by measuring the
                      binding of Ca(2+) to the following five constructs related
                      to GARPs of rod photoreceptors: a 32-mer peptide containing
                      22 carboxylate groups, polyglutamic acid, a recombinant
                      segment comprising 73 carboxylate groups (GLU), GARP1, and
                      GARP2. Ca(2+) binding was investigated by means of a
                      Ca(2+)-sensitive electrode. In all cases, Ca(2+) binds with
                      low affinity; the half-maximum binding constant K(1/2)
                      ranges from 6 to 16 mM. The binding stoichiometry between
                      Ca(2+) ions and carboxylic groups is approximately 1:1; an
                      exception is GARP2, where a binding stoichiometry of
                      approximately 1:2 was found. Hydrodynamic radii of 1.6, 2.8,
                      3.3, 5.7, and 6.7 nm were determined by dynamic light
                      scattering for the 32-mer, polyglutamic acid, GLU, GARP2,
                      and GARP1 constructs, respectively. These results suggest
                      that the peptides as well as GARP1 and GARP2 do not adopt
                      compact globular structures. We conclude that the structures
                      should be regarded as loose coils with low-affinity,
                      high-capacity Ca(2+) binding.},
      keywords     = {Binding Sites / Calcium: chemistry / Glutamic Acid:
                      chemistry / Nerve Tissue Proteins: chemistry / Peptides:
                      chemistry / Protein Binding / Retinal Rod Photoreceptor
                      Cells: chemistry / Nerve Tissue Proteins (NLM Chemicals) /
                      Peptides (NLM Chemicals) / Glutamic Acid (NLM Chemicals) /
                      Calcium (NLM Chemicals) / J (WoSType)},
      cin          = {ICG-4 / INB-1 / INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB793 / I:(DE-Juel1)VDB804 /
                      I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17218469},
      pmc          = {pmc:PMC1852358},
      UT           = {WOS:000245544100028},
      doi          = {10.1529/biophysj.106.094847},
      url          = {https://juser.fz-juelich.de/record/56497},
}