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| Home > Publications database > Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase > print |
| 001 | 32543 | ||
| 005 | 20200402210547.0 | ||
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bbamem.2003.10.007 |
| 024 | 7 | _ | |2 WOS |a WOS:000187163700008 |
| 037 | _ | _ | |a PreJuSER-32543 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |a Poetsch, A. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase |
| 260 | _ | _ | |a Amsterdam |b Elsevier |c 2003 |
| 300 | _ | _ | |a 59 - 66 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a BBA - Biomembranes |x 0005-2736 |0 19423 |v 1618 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a 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. |
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| 588 | _ | _ | |a Dataset connected to Web of Science |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a membrane protein |
| 653 | 2 | 0 | |2 Author |a MALDI mass spectrometry |
| 653 | 2 | 0 | |2 Author |a FTIR |
| 653 | 2 | 0 | |2 Author |a CD spectroscopy |
| 700 | 1 | _ | |a Rexroth, S. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Heberle, J. |b 2 |u FZJ |0 P:(DE-Juel1)VDB572 |
| 700 | 1 | _ | |a Link, T. A. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Dencher, N. A. |b 4 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Seelert, H. |b 5 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |a 10.1016/j.bbamem.2003.10.007 |g Vol. 1618, p. 59 - 66 |p 59 - 66 |q 1618<59 - 66 |0 PERI:(DE-600)2209384-9 |t Biochimica et biophysica acta / Biomembranes |v 1618 |y 2003 |x 0005-2736 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.bbamem.2003.10.007 |
| 909 | C | O | |o oai:juser.fz-juelich.de:32543 |p VDB |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2003 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)35330 |
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| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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