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000032543 0247_ $$2DOI$$a10.1016/j.bbamem.2003.10.007
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000032543 084__ $$2WoS$$aBiochemistry & Molecular Biology
000032543 084__ $$2WoS$$aBiophysics
000032543 1001_ $$0P:(DE-HGF)0$$aPoetsch, A.$$b0
000032543 245__ $$aCharacterisation of subunit II and its oligomer from spinach chloroplast ATP synthase
000032543 260__ $$aAmsterdam$$bElsevier$$c2003
000032543 300__ $$a59 - 66
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000032543 520__ $$aProton ATP synthases carry out energy conversion in mitochondria, chloroplasts, and bacteria. A key element of the membrane integral motor CFO in chloroplasts is the oligomer of subunit III: it converts the energy of a transmembrane electrochemical proton gradient into rotational movement. To enlighten prominent features of the structure-function relationship of subunit III from spinach chloroplasts, new isolation methods were established to obtain highly pure monomeric and oligomeric subunit III in milligram quantities. By Fourier-transform infrared (FTIR) and CD spectroscopy, the predominantly a-helical secondary structure of subunit III was demonstrated. For monomeric subunit III, a conformational change was observed when diluting the SDS-solubilized protein. Under the same conditions the conformation of the oligomer III did not change. A mass of 8003 Da for the monomeric subunit III was determined by MALDI mass spectrometry (MALDI-MS), showing that no posttranslational modifications occurred. By ionisation during MALDI-MS, the noncovalent homooligomer III14 disaggregated into its III monomers. (C) 2003 Elsevier B.V All rights reserved.
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000032543 65320 $$2Author$$amembrane protein
000032543 65320 $$2Author$$aMALDI mass spectrometry
000032543 65320 $$2Author$$aFTIR
000032543 65320 $$2Author$$aCD spectroscopy
000032543 7001_ $$0P:(DE-HGF)0$$aRexroth, S.$$b1
000032543 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b2$$uFZJ
000032543 7001_ $$0P:(DE-HGF)0$$aLink, T. A.$$b3
000032543 7001_ $$0P:(DE-HGF)0$$aDencher, N. A.$$b4
000032543 7001_ $$0P:(DE-HGF)0$$aSeelert, H.$$b5
000032543 773__ $$0PERI:(DE-600)2209384-9$$a10.1016/j.bbamem.2003.10.007$$gVol. 1618, p. 59 - 66$$p59 - 66$$q1618<59 - 66$$tBiochimica et biophysica acta / Biomembranes$$v1618$$x0005-2736$$y2003
000032543 8567_ $$uhttp://dx.doi.org/10.1016/j.bbamem.2003.10.007
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