Hauptseite > Publikationsdatenbank > Effects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex > print

001     51327
005     20200402210131.0
024 7 _ |2 pmid
|a pmid:16410012
024 7 _ |2 DOI
|a 10.1016/j.jmb.2005.12.015
024 7 _ |2 WOS
|a WOS:000235432400013
037 _ _ |a PreJuSER-51327
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Klare, J. P.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Effects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex
260 _ _ |a Amsterdam [u.a.]
|b Elsevier
|c 2006
300 _ _ |a 1207 - 1221
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 Molecular Biology
|x 0022-2836
|0 3552
|v 356
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Lipid-protein interactions are known to play a crucial role in structure and physiological activity of integral membrane proteins. However, current technology for membrane protein purification necessitates extraction from the membrane into detergent micelles. Also, due to experimental protocols, most of the data available for membrane proteins is obtained using detergent-solubilized samples. Stable solubilization of membrane proteins is therefore an important issue in biotechnology as well as in biochemistry and structural biology. An understanding of solubilization effects on structural and functional properties of specific proteins is of utmost relevance for the evaluation and interpretation of experimental results. In this study, a comparison of structural and kinetic data obtained for the archaebacterial photoreceptor/transducer complex from Natronomonas pharaonis (NpSRII/NpHtrII) in detergent-solubilized and lipid-reconstituted states is presented. Laser flash photolysis, fluorescence spectroscopy, and electron paramagnetic resonance spectroscopy data reveal considerable influence of solubilization on the photocycle kinetics of the receptor protein and on the structure of the transducer protein. Especially the protein-membrane proximal region and the protein-protein interfacial domains are sensitive towards non-native conditions. These data demonstrate that relevance of biochemical and structural information obtained from solubilized membrane proteins or membrane protein complexes has to be evaluated carefully.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Archaeal Proteins: chemistry
650 _ 2 |2 MeSH
|a Archaeal Proteins: genetics
650 _ 2 |2 MeSH
|a Archaeal Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Archaeal Proteins: metabolism
650 _ 2 |2 MeSH
|a Detergents: chemistry
650 _ 2 |2 MeSH
|a Electron Spin Resonance Spectroscopy
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Lipids: chemistry
650 _ 2 |2 MeSH
|a Micelles
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Multiprotein Complexes
650 _ 2 |2 MeSH
|a Natronobacterium: chemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: chemistry
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: genetics
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: isolation & purification
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: metabolism
650 _ 2 |2 MeSH
|a Spin Labels
650 _ 7 |0 0
|2 NLM Chemicals
|a Archaeal Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Detergents
650 _ 7 |0 0
|2 NLM Chemicals
|a Lipids
650 _ 7 |0 0
|2 NLM Chemicals
|a Micelles
650 _ 7 |0 0
|2 NLM Chemicals
|a Multiprotein Complexes
650 _ 7 |0 0
|2 NLM Chemicals
|a Sensory Rhodopsins
650 _ 7 |0 0
|2 NLM Chemicals
|a Spin Labels
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a phoborhodopsin
653 2 0 |2 Author
|a phototaxis
653 2 0 |2 Author
|a membrane proteins
653 2 0 |2 Author
|a site-directed spin labeling EPR
653 2 0 |2 Author
|a detergents
700 1 _ |a Bordignon, E.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Doebber, M.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Fitter, J.
|b 3
|u FZJ
|0 P:(DE-Juel1)131961
700 1 _ |a Kriegsmann, J.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB60877
700 1 _ |a Chizhov, I.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Steinhoff, H.-J.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Engelhard, M.
|b 7
|0 P:(DE-HGF)0
773 _ _ |a 10.1016/j.jmb.2005.12.015
|g Vol. 356, p. 1207 - 1221
|p 1207 - 1221
|q 356<1207 - 1221
|0 PERI:(DE-600)1355192-9
|t Journal of molecular biology
|v 356
|y 2006
|x 0022-2836
856 7 _ |u http://dx.doi.org/10.1016/j.jmb.2005.12.015
909 C O |o oai:juser.fz-juelich.de:51327
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
914 1 _ |y 2006
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)80520
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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