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| Home > Publications database > Application of different surface plasmon resonance biosensor chips to monitor the interaction of the CaM-binding site of nitric oxide synthase I and calmodulin > print |
| Home > Publications database > Application of different surface plasmon resonance biosensor chips to monitor the interaction of the CaM-binding site of nitric oxide synthase I and calmodulin > print |
| 001 | 46868 | ||
| 005 | 20200402205958.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:11444865 |
| 024 | 7 | _ | |2 DOI |a 10.1006/bbrc.2001.5206 |
| 024 | 7 | _ | |2 WOS |a WOS:000170020900046 |
| 037 | _ | _ | |a PreJuSER-46868 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |a Fischer, T. |0 P:(DE-Juel1)VDB393 |b 0 |u FZJ |
| 245 | _ | _ | |a Application of different surface plasmon resonance biosensor chips to monitor the interaction of the CaM-binding site of nitric oxide synthase I and calmodulin |
| 260 | _ | _ | |a Orlando, Fla. |b Academic Press |c 2001 |
| 300 | _ | _ | |a 463 - 469 |
| 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 Biochemical and Biophysical Research Communications |x 0006-291X |0 787 |v 285 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Surface plasmon resonance biosensors depend on modified gold surfaces to allow immobilization of proteins or peptides for interaction analysis. We investigated sensor chip surfaces that differ in the geometry of the immobilization matrix: two contain a three-dimensional coupling matrix and two have a surface with immobilization sites on a two-dimensional plane. Properties of sensor chips were compared by studying the interaction of calmodulin with a peptide representing the calmodulin-binding site of nitric oxide synthase I. Apparent K(D) values were determined by three different procedures in order to apply tests for self-consistency. At low surface densities (5-8 fmol/mm(2)) on three of the four tested surfaces, estimated K(D) values were within one order of magnitude and similar to the value found in solution (K(D) = 1-3 nM). When immobilization densities were increased by one to two orders of magnitude, apparent association rate constants were less distorted on a flat carboxymethylated surface than on dextran-coated sensor chips. |
| 536 | _ | _ | |a Zelluläre Signalverarbeitung |c 42.20.1 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK95 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Amino Acid Sequence |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Biosensing Techniques |
| 650 | _ | 2 | |2 MeSH |a Calmodulin: chemistry |
| 650 | _ | 2 | |2 MeSH |a Calmodulin: metabolism |
| 650 | _ | 2 | |2 MeSH |a Kinetics |
| 650 | _ | 2 | |2 MeSH |a Molecular Sequence Data |
| 650 | _ | 2 | |2 MeSH |a Nitric Oxide Synthase: chemistry |
| 650 | _ | 2 | |2 MeSH |a Nitric Oxide Synthase: metabolism |
| 650 | _ | 2 | |2 MeSH |a Nitric Oxide Synthase Type I |
| 650 | _ | 2 | |2 MeSH |a Peptides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Peptides: metabolism |
| 650 | _ | 2 | |2 MeSH |a Rats |
| 650 | _ | 2 | |2 MeSH |a Surface Plasmon Resonance: methods |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Calmodulin |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Peptides |
| 650 | _ | 7 | |0 EC 1.14.13.39 |2 NLM Chemicals |a Nitric Oxide Synthase |
| 650 | _ | 7 | |0 EC 1.14.13.39 |2 NLM Chemicals |a Nitric Oxide Synthase Type I |
| 650 | _ | 7 | |0 EC 1.14.13.39 |2 NLM Chemicals |a Nos1 protein, rat |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a surface plasmon resonance |
| 653 | 2 | 0 | |2 Author |a biosensor surfaces |
| 653 | 2 | 0 | |2 Author |a protein-peptide interaction |
| 653 | 2 | 0 | |2 Author |a calmodulin |
| 653 | 2 | 0 | |2 Author |a nitric oxide synthase |
| 700 | 1 | _ | |a Beyermann, M. |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Koch, K.-W. |0 P:(DE-Juel1)VDB789 |b 2 |u FZJ |
| 773 | _ | _ | |a 10.1006/bbrc.2001.5206 |g Vol. 285, p. 463 - 469 |p 463 - 469 |q 285<463 - 469 |0 PERI:(DE-600)1461396-7 |t Biochemical and biophysical research communications |v 285 |y 2001 |x 0006-291X |
| 909 | C | O | |o oai:juser.fz-juelich.de:46868 |p VDB |
| 913 | 1 | _ | |k 42.20.1 |v Zelluläre Signalverarbeitung |l Biologische Informationsverarbeitung |b Lebenswissenschaften |0 G:(DE-Juel1)FUEK95 |x 0 |
| 914 | 1 | _ | |y 2001 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-1 |l Zelluläre Signalverarbeitung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB57 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)975 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-4-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-1-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-4-20110106 |
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