| Hauptseite > Publikationsdatenbank > Nanodiscs allow the use of integral membrane proteins as analytes in surface plasmon resonance studies > print |
| 001 | 11819 | ||
| 005 | 20200402205918.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:20804721 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.ab.2010.08.028 |
| 024 | 7 | _ | |2 WOS |a WOS:000283886600007 |
| 037 | _ | _ | |a PreJuSER-11819 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemical Research Methods |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Chemistry, Analytical |
| 100 | 1 | _ | |a Glück, J.M. |b 0 |u FZJ |0 P:(DE-Juel1)VDB89237 |
| 245 | _ | _ | |a Nanodiscs allow the use of integral membrane proteins as analytes in surface plasmon resonance studies |
| 260 | _ | _ | |a San Diego, Calif. |b Elsevier |c 2011 |
| 300 | _ | _ | |a 46 - 52 |
| 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 Analytical Biochemistry |x 0003-2697 |0 362 |y 1 |v 408 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Nanodiscs are small-sized and flat model membranes that provide a close to native environment for reconstitution of integral membrane proteins. Incorporation of membrane proteins into nanodiscs results in water-soluble proteolipid particles making the membrane proteins amenable to a multitude of bioanalytical techniques originally developed for soluble proteins. The transmembrane domain of the human CD4 receptor was fused to ubiquitin with a preceding N-terminal decahistidine tag. The resulting integral membrane protein was incorporated into nanodiscs. Binding of the nanodisc-inserted histidine-tagged protein to a monoclonal anti-pentahistidine antibody was quantified using surface plasmon resonance (SPR) experiments. For the first time, a membrane-inserted transmembrane protein was employed as analyte while the antibody served as ligand immobilized on the sensor chip surface. SPR experiments were conducted in single-cycle mode. We demonstrate that the nanodisc-incorporated membrane protein showed nearly identical affinity toward the antibody as did the soluble decahistidine-tagged ubiquitin studied in a comparative experiment. Advantages of the new experimental setup and potential applications are discussed. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 536 | _ | _ | |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |0 G:(DE-Juel1)FUEK505 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Antibodies, Monoclonal: immunology |
| 650 | _ | 2 | |2 MeSH |a Antigens, CD4: chemistry |
| 650 | _ | 2 | |2 MeSH |a Antigens, CD4: genetics |
| 650 | _ | 2 | |2 MeSH |a Antigens, CD4: metabolism |
| 650 | _ | 2 | |2 MeSH |a Biosensing Techniques: methods |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Kinetics |
| 650 | _ | 2 | |2 MeSH |a Membrane Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Membrane Proteins: genetics |
| 650 | _ | 2 | |2 MeSH |a Membrane Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Nanostructures: chemistry |
| 650 | _ | 2 | |2 MeSH |a Oligopeptides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Oligopeptides: genetics |
| 650 | _ | 2 | |2 MeSH |a Oligopeptides: metabolism |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Recombinant Fusion Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Recombinant Fusion Proteins: genetics |
| 650 | _ | 2 | |2 MeSH |a Recombinant Fusion Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Surface Plasmon Resonance: methods |
| 650 | _ | 2 | |2 MeSH |a Ubiquitin: chemistry |
| 650 | _ | 2 | |2 MeSH |a Ubiquitin: genetics |
| 650 | _ | 2 | |2 MeSH |a Ubiquitin: metabolism |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Antibodies, Monoclonal |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Antigens, CD4 |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Membrane Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Oligopeptides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Recombinant Fusion Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Ubiquitin |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a Surface plasmon resonance |
| 653 | 2 | 0 | |2 Author |a Biacore |
| 653 | 2 | 0 | |2 Author |a Single-cycle kinetics |
| 653 | 2 | 0 | |2 Author |a Nanodisc |
| 700 | 1 | _ | |a Koenig, B. W. |b 1 |u FZJ |0 P:(DE-Juel1)132009 |
| 700 | 1 | _ | |a Willbold, D. |b 2 |u FZJ |0 P:(DE-Juel1)132029 |
| 773 | _ | _ | |a 10.1016/j.ab.2010.08.028 |g Vol. 408, p. 46 - 52 |p 46 - 52 |q 408<46 - 52 |0 PERI:(DE-600)1461105-3 |t Analytical biochemistry |v 408 |y 2011 |x 0003-2697 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.ab.2010.08.028 |
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| 914 | 1 | _ | |y 2011 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
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