Home > Publications database > 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
909 C O |o oai:juser.fz-juelich.de:11819
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|v Functional Macromolecules and Complexes
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914 1 _ |y 2011
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k ICS-6
|l Strukturbiochemie
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