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@ARTICLE{Poetsch:32543,
      author       = {Poetsch, A. and Rexroth, S. and Heberle, J. and Link, T. A.
                      and Dencher, N. A. and Seelert, H.},
      title        = {{C}haracterisation of subunit {II} and its oligomer from
                      spinach chloroplast {ATP} synthase},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1618},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-32543},
      pages        = {59 - 66},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Proton ATP synthases carry out energy conversion in
                      mitochondria, chloroplasts, and bacteria. A key element of
                      the membrane integral motor CFO in chloroplasts is the
                      oligomer of subunit III: it converts the energy of a
                      transmembrane electrochemical proton gradient into
                      rotational movement. To enlighten prominent features of the
                      structure-function relationship of subunit III from spinach
                      chloroplasts, new isolation methods were established to
                      obtain highly pure monomeric and oligomeric subunit III in
                      milligram quantities. By Fourier-transform infrared (FTIR)
                      and CD spectroscopy, the predominantly a-helical secondary
                      structure of subunit III was demonstrated. For monomeric
                      subunit III, a conformational change was observed when
                      diluting the SDS-solubilized protein. Under the same
                      conditions the conformation of the oligomer III did not
                      change. A mass of 8003 Da for the monomeric subunit III was
                      determined by MALDI mass spectrometry (MALDI-MS), showing
                      that no posttranslational modifications occurred. By
                      ionisation during MALDI-MS, the noncovalent homooligomer
                      III14 disaggregated into its III monomers. (C) 2003 Elsevier
                      B.V All rights reserved.},
      keywords     = {J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000187163700008},
      doi          = {10.1016/j.bbamem.2003.10.007},
      url          = {https://juser.fz-juelich.de/record/32543},
}