Hauptseite > Publikationsdatenbank > Electrochemically induced Surface Enhanced Infrared Difference Absorption (SEIDA) spectroscopy of a protein monolayer > print

001     28975
005     20200423203454.0
024 7 _ |a pmid:12708842
|2 pmid
024 7 _ |a 10.1021/ja0346532
|2 DOI
024 7 _ |a WOS:000182491700014
|2 WOS
024 7 _ |a 2128/696
|2 Handle
037 _ _ |a PreJuSER-28975
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Chemistry, Multidisciplinary
100 1 _ |a Ataka, K.
|0 P:(DE-Juel1)VDB5396
|b 0
|u FZJ
245 _ _ |a Electrochemically induced Surface Enhanced Infrared Difference Absorption (SEIDA) spectroscopy of a protein monolayer
260 _ _ |a Washington, DC
|b American Chemical Society
|c 2003
300 _ _ |a 4986 - 4987
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 Journal of the American Chemical Society
|x 0002-7863
|0 8502
|v 125
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Functional infrared difference spectra of a protein monolayer are recorded by exploiting the surface enhancement exerted by a modified gold surface. The noble metal is used as the working electrode to induce redox-linked structural changes in the single layer of cytochrome c. The observed differences in the relative band intensities as compared to the difference spectrum of cytochrome c in solution are attributed to orientational effects of the adsorbed protein.
536 _ _ |a Neurowissenschaften
|c L01
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cytochrome c Group: chemistry
650 _ 2 |2 MeSH
|a Cytochrome c Group: metabolism
650 _ 2 |2 MeSH
|a Electrochemistry: methods
650 _ 2 |2 MeSH
|a Horses
650 _ 2 |2 MeSH
|a Myocardium: chemistry
650 _ 2 |2 MeSH
|a Oxidation-Reduction
650 _ 2 |2 MeSH
|a Spectrophotometry, Infrared: methods
650 _ 2 |2 MeSH
|a Surface Properties
650 _ 7 |0 0
|2 NLM Chemicals
|a Cytochrome c Group
650 _ 7 |a J
|2 WoSType
700 1 _ |a Heberle, J.
|0 P:(DE-Juel1)VDB572
|b 1
|u FZJ
773 _ _ |a 10.1021/ja0346532
|g Vol. 125, p. 4986 - 4987
|p 4986 - 4987
|q 125<4986 - 4987
|0 PERI:(DE-600)1472210-0
|t Journal of the American Chemical Society
|v 125
|y 2003
|x 0002-7863
856 7 _ |u http://dx.doi.org/10.1021/ja0346532
|u http://hdl.handle.net/2128/696
856 4 _ |u https://juser.fz-juelich.de/record/28975/files/24624.pdf
|y OpenAccess
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909 C O |o oai:juser.fz-juelich.de:28975
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913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
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914 1 _ |y 2003
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
915 _ _ |2 StatID
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|a OpenAccess
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)24624
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