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000051327 0247_ $$2DOI$$a10.1016/j.jmb.2005.12.015
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000051327 041__ $$aeng
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000051327 084__ $$2WoS$$aBiochemistry & Molecular Biology
000051327 1001_ $$0P:(DE-HGF)0$$aKlare, J. P.$$b0
000051327 245__ $$aEffects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex
000051327 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2006
000051327 300__ $$a1207 - 1221
000051327 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000051327 3367_ $$2BibTeX$$aARTICLE
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000051327 440_0 $$03552$$aJournal of Molecular Biology$$v356$$x0022-2836
000051327 500__ $$aRecord converted from VDB: 12.11.2012
000051327 520__ $$aLipid-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.
000051327 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000051327 588__ $$aDataset connected to Web of Science, Pubmed
000051327 650_2 $$2MeSH$$aArchaeal Proteins: chemistry
000051327 650_2 $$2MeSH$$aArchaeal Proteins: genetics
000051327 650_2 $$2MeSH$$aArchaeal Proteins: isolation & purification
000051327 650_2 $$2MeSH$$aArchaeal Proteins: metabolism
000051327 650_2 $$2MeSH$$aDetergents: chemistry
000051327 650_2 $$2MeSH$$aElectron Spin Resonance Spectroscopy
000051327 650_2 $$2MeSH$$aLight
000051327 650_2 $$2MeSH$$aLipids: chemistry
000051327 650_2 $$2MeSH$$aMicelles
000051327 650_2 $$2MeSH$$aModels, Molecular
000051327 650_2 $$2MeSH$$aMultiprotein Complexes
000051327 650_2 $$2MeSH$$aNatronobacterium: chemistry
000051327 650_2 $$2MeSH$$aProtein Conformation
000051327 650_2 $$2MeSH$$aSensory Rhodopsins: chemistry
000051327 650_2 $$2MeSH$$aSensory Rhodopsins: genetics
000051327 650_2 $$2MeSH$$aSensory Rhodopsins: isolation & purification
000051327 650_2 $$2MeSH$$aSensory Rhodopsins: metabolism
000051327 650_2 $$2MeSH$$aSpin Labels
000051327 650_7 $$00$$2NLM Chemicals$$aArchaeal Proteins
000051327 650_7 $$00$$2NLM Chemicals$$aDetergents
000051327 650_7 $$00$$2NLM Chemicals$$aLipids
000051327 650_7 $$00$$2NLM Chemicals$$aMicelles
000051327 650_7 $$00$$2NLM Chemicals$$aMultiprotein Complexes
000051327 650_7 $$00$$2NLM Chemicals$$aSensory Rhodopsins
000051327 650_7 $$00$$2NLM Chemicals$$aSpin Labels
000051327 650_7 $$2WoSType$$aJ
000051327 65320 $$2Author$$aphoborhodopsin
000051327 65320 $$2Author$$aphototaxis
000051327 65320 $$2Author$$amembrane proteins
000051327 65320 $$2Author$$asite-directed spin labeling EPR
000051327 65320 $$2Author$$adetergents
000051327 7001_ $$0P:(DE-HGF)0$$aBordignon, E.$$b1
000051327 7001_ $$0P:(DE-HGF)0$$aDoebber, M.$$b2
000051327 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b3$$uFZJ
000051327 7001_ $$0P:(DE-Juel1)VDB60877$$aKriegsmann, J.$$b4$$uFZJ
000051327 7001_ $$0P:(DE-HGF)0$$aChizhov, I.$$b5
000051327 7001_ $$0P:(DE-HGF)0$$aSteinhoff, H.-J.$$b6
000051327 7001_ $$0P:(DE-HGF)0$$aEngelhard, M.$$b7
000051327 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2005.12.015$$gVol. 356, p. 1207 - 1221$$p1207 - 1221$$q356<1207 - 1221$$tJournal of molecular biology$$v356$$x0022-2836$$y2006
000051327 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2005.12.015
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000051327 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000051327 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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