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@ARTICLE{Klare:51327,
      author       = {Klare, J. P. and Bordignon, E. and Doebber, M. and Fitter,
                      J. and Kriegsmann, J. and Chizhov, I. and Steinhoff, H.-J.
                      and Engelhard, M.},
      title        = {{E}ffects of {S}olubilization on the {S}tructure and
                      {F}unction of the {S}ensory {R}hodopsin {II}/{T}ransducer
                      {C}omplex},
      journal      = {Journal of molecular biology},
      volume       = {356},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-51327},
      pages        = {1207 - 1221},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Archaeal Proteins: chemistry / Archaeal Proteins: genetics
                      / Archaeal Proteins: isolation $\&$ purification / Archaeal
                      Proteins: metabolism / Detergents: chemistry / Electron Spin
                      Resonance Spectroscopy / Light / Lipids: chemistry /
                      Micelles / Models, Molecular / Multiprotein Complexes /
                      Natronobacterium: chemistry / Protein Conformation / Sensory
                      Rhodopsins: chemistry / Sensory Rhodopsins: genetics /
                      Sensory Rhodopsins: isolation $\&$ purification / Sensory
                      Rhodopsins: metabolism / Spin Labels / Archaeal Proteins
                      (NLM Chemicals) / Detergents (NLM Chemicals) / Lipids (NLM
                      Chemicals) / Micelles (NLM Chemicals) / Multiprotein
                      Complexes (NLM Chemicals) / Sensory Rhodopsins (NLM
                      Chemicals) / Spin Labels (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16410012},
      UT           = {WOS:000235432400013},
      doi          = {10.1016/j.jmb.2005.12.015},
      url          = {https://juser.fz-juelich.de/record/51327},
}