% 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{Poetsch:59160,
      author       = {Poetsch, A. and Berzborn, R. J. and Heberle, J. and Link,
                      T. A. and Dencher, N. A. and Seelert, H.},
      title        = {{B}iophysics and {B}ioinformatics {R}eveal {S}tructural
                      {D}ifferences of the {T}wo {P}eripheral {S}talk {S}ubunits
                      in {C}hloroplast {ATP} {S}ynthase},
      journal      = {Journal of biochemistry},
      volume       = {141},
      issn         = {0021-924x},
      address      = {Tokyo},
      publisher    = {Soc.},
      reportid     = {PreJuSER-59160},
      pages        = {411 - 420},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {ATP synthases convert an electrochemical proton gradient
                      into rotational movement to produce the ubiquitous energy
                      currency adenosine triphosphate. Tension generated by the
                      rotational torque is compensated by the stator. For this
                      task, a peripheral stalk flexibly fixes the hydrophilic
                      catalytic part F1 to the membrane integral proton conducting
                      part F(O) of the ATP synthase. While in eubacteria a
                      homodimer of b subunits forms the peripheral stalk, plant
                      chloroplasts and cyanobacteria possess a heterodimer of
                      subunits I and II. To better understand the functional and
                      structural consequences of this unique feature of
                      photosynthetic ATP synthases, a procedure was developed to
                      purify subunit I from spinach chloroplasts. The secondary
                      structure of subunit I, which is not homologous to bacterial
                      b subunits, was compared to heterologously expressed subunit
                      II using CD and FTIR spectroscopy. The content of
                      alpha-helix was determined by CD spectroscopy to $67\%$ for
                      subunit I and $41\%$ for subunit II. In addition,
                      bioinformatics was applied to predict the secondary
                      structure of the two subunits and the location of the
                      putative coiled-coil dimerization regions. Three helical
                      domains were predicted for subunit I and only two
                      uninterrupted domains for the shorter subunit II. The
                      predicted length of coiled-coil regions varied between
                      different species and between subunits I and II.},
      keywords     = {Amino Acid Sequence / Biophysical Phenomena / Biophysics /
                      Chloroplast Proton-Translocating ATPases: chemistry /
                      Computational Biology / Molecular Sequence Data / Protein
                      Structure, Secondary / Protein Subunits: chemistry /
                      Sequence Alignment / Spectroscopy, Fourier Transform
                      Infrared / Spinacia oleracea: enzymology / Protein Subunits
                      (NLM Chemicals) / Chloroplast Proton-Translocating ATPases
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17283010},
      UT           = {WOS:000245676800013},
      doi          = {10.1093/jb/mvm045},
      url          = {https://juser.fz-juelich.de/record/59160},
}