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001     38377
005     20200402205427.0
024 7 _ |2 pmid
|a pmid:15185365
024 7 _ |2 DOI
|a 10.1002/cbic.200300687
024 7 _ |2 WOS
|a WOS:000220773500004
037 _ _ |a PreJuSER-38377
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Chemistry, Medicinal
100 1 _ |a Nyquist, R. M.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a The molecular mechanism of membrane proteins probed by evanescent infrared waves
260 _ _ |a Weinheim
|b Wiley-VCH
|c 2004
300 _ _ |a 431 - 436
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 ChemBioChem
|x 1439-4227
|0 8962
|y 4
|v 5
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The catalytic action of membrane proteins is vital to many cellular processes. Yet the molecular mechanisms remain poorly understood. We describe here the technique of evanescent infrared difference spectroscopy as a tool to decipher the structural changes associated with the enzymatic action of membrane proteins. Functional changes as minute as the protonation state of individual amino acid side chains can be observed and linked to interactions with a ligand, agonist, effector, or redox partner.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
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|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: chemistry
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: metabolism
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: chemistry
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: metabolism
650 _ 2 |2 MeSH
|a Membrane Proteins: chemistry
650 _ 2 |2 MeSH
|a Membrane Proteins: metabolism
650 _ 2 |2 MeSH
|a Rhodopsin: chemistry
650 _ 2 |2 MeSH
|a Rhodopsin: metabolism
650 _ 2 |2 MeSH
|a Spectrophotometry, Infrared: methods
650 _ 7 |0 0
|2 NLM Chemicals
|a Membrane Proteins
650 _ 7 |0 53026-44-1
|2 NLM Chemicals
|a Bacteriorhodopsins
650 _ 7 |0 9009-81-8
|2 NLM Chemicals
|a Rhodopsin
650 _ 7 |0 EC 1.9.3.1
|2 NLM Chemicals
|a Electron Transport Complex IV
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a attenuated total reflection spectroscopy
653 2 0 |2 Author
|a bacteriorhodopsin
653 2 0 |2 Author
|a cytochrome c oxidase
653 2 0 |2 Author
|a IR spectroscopy
653 2 0 |2 Author
|a membrane proteins
653 2 0 |2 Author
|a reaction mechanisms
700 1 _ |a Ataka, K.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB5396
700 1 _ |a Heberle, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB572
773 _ _ |a 10.1002/cbic.200300687
|g Vol. 5, p. 431 - 436
|p 431 - 436
|q 5<431 - 436
|0 PERI:(DE-600)2020469-3
|t ChemBioChem
|v 5
|y 2004
|x 1439-4227
856 7 _ |u http://dx.doi.org/10.1002/cbic.200300687
909 C O |o oai:juser.fz-juelich.de:38377
|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 2004
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)49047
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
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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