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Volumn 13, Issue 5, 2008, Pages 338-350

Strategies to prepare and characterize native membrane proteins and protein membranes by AFM

Author keywords

Atomic force microscopy; Compartments; Molecular interactions; Native protein membranes; Polymer supported membranes; Protein assembly; Single molecule force spectroscopy; Structure and function relationship; Tethered membranes

Indexed keywords

ATOMIC FORCE MICROSCOPY; BIOLOGICAL MEMBRANES; CELL MEMBRANES; CELLS; CYTOLOGY; FLOW INTERACTIONS; MEMBRANES; MICROSCOPIC EXAMINATION; NEURAL NETWORKS; PROTEINS; RELIABILITY; SCANNING PROBE MICROSCOPY;

EID: 41149164202     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cocis.2007.09.002     Document Type: Review
Times cited : (54)

References (66)
  • 1
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 2
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman D.M. Membranes are more mosaic than fluid. Nature 438 (2005) 578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 3
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A., and Müller D.J. Observing single biomolecules at work with the atomic force microscope. Nat Struct Biol 7 (2000) 715-718
    • (2000) Nat Struct Biol , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 4
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated Connexin26 gap junctions
    • Müller D.J., Hand G.M., Engel A., and Sosinsky G. Conformational changes in surface structures of isolated Connexin26 gap junctions. EMBO J 21 (2002) 3598-3607
    • (2002) EMBO J , vol.21 , pp. 3598-3607
    • Müller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.4
  • 5
    • 34247863710 scopus 로고    scopus 로고
    • Aminosulfonate modulated pH-induced conformational changes in Connexin26 hemichannels
    • 'Gap junction channels regulate cell-cell communication by passing metabolites, ions, and signaling molecules. AFM topographs recorded in the presence of aminosulfonate, a cellular compound, show that gap junction hemichannels exhibit an open entrance at pH 7.6, which gradually closes with decreasing pH. At pH 6.0 the channel is fully closed. The structural data explain a physiologically observed gating behavior of gap junction hemichannels.'
    • Yu J., Bippes C.A., Hand G.M., Muller D.J., and Sosinsky G.E. Aminosulfonate modulated pH-induced conformational changes in Connexin26 hemichannels. J Biol Chem 282 (2007) 8895-8904. 'Gap junction channels regulate cell-cell communication by passing metabolites, ions, and signaling molecules. AFM topographs recorded in the presence of aminosulfonate, a cellular compound, show that gap junction hemichannels exhibit an open entrance at pH 7.6, which gradually closes with decreasing pH. At pH 6.0 the channel is fully closed. The structural data explain a physiologically observed gating behavior of gap junction hemichannels.'
    • (2007) J Biol Chem , vol.282 , pp. 8895-8904
    • Yu, J.1    Bippes, C.A.2    Hand, G.M.3    Muller, D.J.4    Sosinsky, G.E.5
  • 8
    • 0347717833 scopus 로고    scopus 로고
    • Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy
    • 'AFM resolves the supramolecular arrangement of the photosynthetic system from Rsp rubrum. Nanodissection of the reaction center (RC) by the AFM tip removes the RC-H subunit and reveals the underlying RC-L and -M subunits. Light-harvesting1 (LH1) complexes completely lacking the RC were found, providing ideal conditions for imaging both rings of LH1 polypeptides for the first time by AFM. The AFM data has been reconciled with previous electron microscopy and NMR data to produce a model of the RC-LH1 complex.'
    • Fotiadis D., Qian P., Philippsen A., Bullough P.A., Engel A., and Hunter C.N. Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy. J Biol Chem 279 (2004) 2063-2068. 'AFM resolves the supramolecular arrangement of the photosynthetic system from Rsp rubrum. Nanodissection of the reaction center (RC) by the AFM tip removes the RC-H subunit and reveals the underlying RC-L and -M subunits. Light-harvesting1 (LH1) complexes completely lacking the RC were found, providing ideal conditions for imaging both rings of LH1 polypeptides for the first time by AFM. The AFM data has been reconciled with previous electron microscopy and NMR data to produce a model of the RC-LH1 complex.'
    • (2004) J Biol Chem , vol.279 , pp. 2063-2068
    • Fotiadis, D.1    Qian, P.2    Philippsen, A.3    Bullough, P.A.4    Engel, A.5    Hunter, C.N.6
  • 9
    • 20444382012 scopus 로고    scopus 로고
    • Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy
    • Scheuring S., Levy D., and Rigaud J.L. Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy. Biochim Biophys Acta 1712 (2005) 109-127
    • (2005) Biochim Biophys Acta , vol.1712 , pp. 109-127
    • Scheuring, S.1    Levy, D.2    Rigaud, J.L.3
  • 10
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: rhodopsin dimers in native disc membranes
    • 'Controversing existing models of rhodopsin assemblies in the native disc membrane of the rod outer segment of the eye, high-resolution AFM observed for the first time that rhodopsin molecules form dimers. Structural and functional implications are briefly discussed.'
    • Fotiadis D., Liang Y., Filipek S., Saperstein D.A., Engel A., and Palczewski K. Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature 421 (2003) 127-128. 'Controversing existing models of rhodopsin assemblies in the native disc membrane of the rod outer segment of the eye, high-resolution AFM observed for the first time that rhodopsin molecules form dimers. Structural and functional implications are briefly discussed.'
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 11
    • 33748578027 scopus 로고    scopus 로고
    • AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes
    • Scheuring S. AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes. Curr Opin Chem Biol 10 (2006) 387-393
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 387-393
    • Scheuring, S.1
  • 12
    • 34249696578 scopus 로고    scopus 로고
    • The supramolecular assemblies of voltage-dependent anion channels in the native membrane
    • 'AFM of the native outer mitochondrial membrane demonstrates that the voltage dependent anion channel (VDAC) assembles into monomers, tetramers, and higher oligomers. Functional importance of these assemblies are discussed.'
    • Hoogenboom B.W., Suda K., Engel A., and Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J Mol Biol 370 (2007) 246-255. 'AFM of the native outer mitochondrial membrane demonstrates that the voltage dependent anion channel (VDAC) assembles into monomers, tetramers, and higher oligomers. Functional importance of these assemblies are discussed.'
    • (2007) J Mol Biol , vol.370 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 13
    • 34247567854 scopus 로고    scopus 로고
    • Supramolecular assembly of VDAC in native mitochondrial outer membranes
    • 'AFM of the native outer mitochondrial membrane observes VDAC. Functional importance of possible assemblies are discussed.'
    • Goncalves R.P., Buzhynskyy N., Prima V., Sturgis J.N., and Scheuring S. Supramolecular assembly of VDAC in native mitochondrial outer membranes. J Mol Biol 369 (2007) 413-418. 'AFM of the native outer mitochondrial membrane observes VDAC. Functional importance of possible assemblies are discussed.'
    • (2007) J Mol Biol , vol.369 , pp. 413-418
    • Goncalves, R.P.1    Buzhynskyy, N.2    Prima, V.3    Sturgis, J.N.4    Scheuring, S.5
  • 14
    • 0033860735 scopus 로고    scopus 로고
    • Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: silane-polyethyleneglycol-lipid as a cushion and covalent linker
    • 'Development of a tethered polymer-supported planar lipid bilayer system. For increased stability of the membrane a silane-polyethyleneglycol-lipid forms a mechanically flexible but covalent linkage to the support. The diffusion of lipids and proteins shows that the polymer-supported bilayer excellently mimics properties of a cellular membrane.'
    • Wagner M.L., and Tamm L.K. Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: silane-polyethyleneglycol-lipid as a cushion and covalent linker. Biophys J 79 (2000) 1400-1414. 'Development of a tethered polymer-supported planar lipid bilayer system. For increased stability of the membrane a silane-polyethyleneglycol-lipid forms a mechanically flexible but covalent linkage to the support. The diffusion of lipids and proteins shows that the polymer-supported bilayer excellently mimics properties of a cellular membrane.'
    • (2000) Biophys J , vol.79 , pp. 1400-1414
    • Wagner, M.L.1    Tamm, L.K.2
  • 15
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • 'This review provides an excellent overview on polymer supported membranes to mimic the cell membrane.'
    • Tanaka M., and Sackmann E. Polymer-supported membranes as models of the cell surface. Nature 437 (2005) 656-663. 'This review provides an excellent overview on polymer supported membranes to mimic the cell membrane.'
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 16
    • 0037066260 scopus 로고    scopus 로고
    • Cell adhesion as wetting transition?
    • Sackmann E., and Bruinsma R.F. Cell adhesion as wetting transition?. ChemPhysChem 3 (2002) 262-269
    • (2002) ChemPhysChem , vol.3 , pp. 262-269
    • Sackmann, E.1    Bruinsma, R.F.2
  • 18
    • 0036619802 scopus 로고    scopus 로고
    • Sampling the conformational space of membrane protein surfaces with the AFM
    • Scheuring S., Müller D.J., Stahlberg H., Engel H.A., and Engel A. Sampling the conformational space of membrane protein surfaces with the AFM. Eur Biophys J 31 (2002) 172-178
    • (2002) Eur Biophys J , vol.31 , pp. 172-178
    • Scheuring, S.1    Müller, D.J.2    Stahlberg, H.3    Engel, H.A.4    Engel, A.5
  • 19
    • 0034698003 scopus 로고    scopus 로고
    • Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence
    • Fotiadis D., Hasler L., Müller D.J., Stahlberg H., Kistler J., and Engel A. Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J Mol Biol 300 (2000) 779-789
    • (2000) J Mol Biol , vol.300 , pp. 779-789
    • Fotiadis, D.1    Hasler, L.2    Müller, D.J.3    Stahlberg, H.4    Kistler, J.5    Engel, A.6
  • 22
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • 'AFM topographs of native membrane preparations extracted from high- and low-light-adapted Rsp. photometricum cells show the supramolecular arrangement of light-harvesting2 (LH2) rings and light-harvesting1 reaction center core complexes. Core complexes of the high-light-adapted photosynthetic apparatus are homogeneously distributed and surrounded by LH2 rings. This ensures sufficiently coupling of the core complexes and rapid energy trapping of excitons. In contrast, core complexes of the low-light-adapted are surrounded by an increased number of LH2 rings forming an almost paracrystalline.'
    • Scheuring S., and Sturgis J.N. Chromatic adaptation of photosynthetic membranes. Science 309 (2005) 484-487. 'AFM topographs of native membrane preparations extracted from high- and low-light-adapted Rsp. photometricum cells show the supramolecular arrangement of light-harvesting2 (LH2) rings and light-harvesting1 reaction center core complexes. Core complexes of the high-light-adapted photosynthetic apparatus are homogeneously distributed and surrounded by LH2 rings. This ensures sufficiently coupling of the core complexes and rapid energy trapping of excitons. In contrast, core complexes of the low-light-adapted are surrounded by an increased number of LH2 rings forming an almost paracrystalline.'
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 23
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller D.J., Amrein M., and Engel A. Adsorption of biological molecules to a solid support for scanning probe microscopy. J Struct Biol 119 (1997) 172-188
    • (1997) J Struct Biol , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 24
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., and Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys J 76 (1999) 1101-1111
    • (1999) Biophys J , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 25
    • 33644782653 scopus 로고    scopus 로고
    • Focus on the living
    • Hogan J. Focus on the living. Nature 440 (2006) 14-15
    • (2006) Nature , vol.440 , pp. 14-15
    • Hogan, J.1
  • 26
    • 33749339997 scopus 로고    scopus 로고
    • Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL
    • Yokokawa M., Wada C., Ando T., Sakai N., Yagi A., Yoshimura S.H., et al. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. Embo J 25 (2006) 4567-4576
    • (2006) Embo J , vol.25 , pp. 4567-4576
    • Yokokawa, M.1    Wada, C.2    Ando, T.3    Sakai, N.4    Yagi, A.5    Yoshimura, S.H.6
  • 27
    • 33846794779 scopus 로고    scopus 로고
    • Breaking the speed limit with atomic force microscopy
    • 'How fast can an AFM capture topographs? By developing two different concepts towards ultra high-speed scanning AFM the group of Mervyn Miles could record up to 1300 frames/s. A high-speed flexure scanning stage mounted under a piezotube holding an AFM cantilever allowed imaging at a video rate of 30 frames/s. The highest imaging speed could be achieved by combining a tuning folk and the high-speed flexure scanning stage.'
    • Picco L.M., Bozec L., Ulcinas A., Engledew D.J., Antognozzi M., Horton M.A., et al. Breaking the speed limit with atomic force microscopy. Nanotechnology 18 (2007) 044030. 'How fast can an AFM capture topographs? By developing two different concepts towards ultra high-speed scanning AFM the group of Mervyn Miles could record up to 1300 frames/s. A high-speed flexure scanning stage mounted under a piezotube holding an AFM cantilever allowed imaging at a video rate of 30 frames/s. The highest imaging speed could be achieved by combining a tuning folk and the high-speed flexure scanning stage.'
    • (2007) Nanotechnology , vol.18 , pp. 044030
    • Picco, L.M.1    Bozec, L.2    Ulcinas, A.3    Engledew, D.J.4    Antognozzi, M.5    Horton, M.A.6
  • 28
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 29
    • 0141757507 scopus 로고    scopus 로고
    • Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase
    • Seelert H., Dencher N.A., and Muller D.J. Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase. J Mol Biol 333 (2003) 337-344
    • (2003) J Mol Biol , vol.333 , pp. 337-344
    • Seelert, H.1    Dencher, N.A.2    Muller, D.J.3
  • 30
    • 27644566520 scopus 로고    scopus 로고
    • The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory
    • Pogoryelov D., Yu J., Meier T., Vonck J., Dimroth P., and Muller D.J. The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory. EMBO Rep 6 (2005) 1040-1044
    • (2005) EMBO Rep , vol.6 , pp. 1040-1044
    • Pogoryelov, D.1    Yu, J.2    Meier, T.3    Vonck, J.4    Dimroth, P.5    Muller, D.J.6
  • 31
    • 33645958615 scopus 로고    scopus 로고
    • Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors
    • 'This review sums up the multiple structural (AFM) and functional studies (see [10]) to characterize the natively occurring rhodopsin dimer. It discusses the biological significance of this finding for G-protein coupled receptors and rhodopsin in detail.'
    • Fotiadis D., Jastrzebska B., Philippsen A., Muller D.J., Palczewski K., and Engel A. Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors. Curr Opin Struct Biol 16 (2006) 252-259. 'This review sums up the multiple structural (AFM) and functional studies (see [10]) to characterize the natively occurring rhodopsin dimer. It discusses the biological significance of this finding for G-protein coupled receptors and rhodopsin in detail.'
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 252-259
    • Fotiadis, D.1    Jastrzebska, B.2    Philippsen, A.3    Muller, D.J.4    Palczewski, K.5    Engel, A.6
  • 32
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller D.J., and Engel A. Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J Mol Biol 285 (1999) 1347-1351
    • (1999) J Mol Biol , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 33
    • 0036828872 scopus 로고    scopus 로고
    • PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding
    • Andersen C., Schiffler B., Charbit A., and Benz R. PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J Biol Chem 277 (2002) 41318-41325
    • (2002) J Biol Chem , vol.277 , pp. 41318-41325
    • Andersen, C.1    Schiffler, B.2    Charbit, A.3    Benz, R.4
  • 34
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • Yildiz O., Vinothkumar K.R., Goswami P., and Kuhlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. Embo J 25 (2006) 3702-3713
    • (2006) Embo J , vol.25 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kuhlbrandt, W.4
  • 35
    • 0041837560 scopus 로고    scopus 로고
    • Single-molecule visualization in cell biology
    • Sako Y., and Yanagida T. Single-molecule visualization in cell biology. Nat Rev Mol Cell Biol Suppl (2003) SS1-SS5
    • (2003) Nat Rev Mol Cell Biol , Issue.SUPPL
    • Sako, Y.1    Yanagida, T.2
  • 36
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • 'Recent approaches of SMFS detecting and locating molecular interactions of membrane proteins is provided. SMFS allows to observe how these molecular interactions drive folding, unfolding, stability, and the functional state of membrane proteins being embedded in their native environment the membrane and exposed to physiological conditions.'
    • Kedrov A., Janovjak H., Sapra K.T., and Muller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu Rev Biophys Biomol Struct 36 (2007) 233-260. 'Recent approaches of SMFS detecting and locating molecular interactions of membrane proteins is provided. SMFS allows to observe how these molecular interactions drive folding, unfolding, stability, and the functional state of membrane proteins being embedded in their native environment the membrane and exposed to physiological conditions.'
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 37
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • 'AFM topographs of native lens membranes resolves the supramolecular architecture of junctional microdomains. In these microdomains AQP0 assembles into two-dimensional crystals surrounded by gap junction hemichannels. It is assumed that hydrophobic mismatch with the lipid bilayer forces AQP0 into this crystalline assembly. Extracellular surface structures of AQP0 suggest that the water pores are in their closed conformation.'
    • Buzhynskyy N., Hite R.K., Walz T., and Scheuring S. The supramolecular architecture of junctional microdomains in native lens membranes. EMBO Rep 8 (2007) 51-55. 'AFM topographs of native lens membranes resolves the supramolecular architecture of junctional microdomains. In these microdomains AQP0 assembles into two-dimensional crystals surrounded by gap junction hemichannels. It is assumed that hydrophobic mismatch with the lipid bilayer forces AQP0 into this crystalline assembly. Extracellular surface structures of AQP0 suggest that the water pores are in their closed conformation.'
    • (2007) EMBO Rep , vol.8 , pp. 51-55
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 38
    • 0032866779 scopus 로고    scopus 로고
    • Direct observation of one-dimensional diffusion and transcription by Escherichia coli RNA polymerase
    • Guthold M., Zhu X., Rivetti C., Yang G., Thomson N.H., Kasas S., et al. Direct observation of one-dimensional diffusion and transcription by Escherichia coli RNA polymerase. Biophys J 77 (1999) 2284-2294
    • (1999) Biophys J , vol.77 , pp. 2284-2294
    • Guthold, M.1    Zhu, X.2    Rivetti, C.3    Yang, G.4    Thomson, N.H.5    Kasas, S.6
  • 39
    • 21344468842 scopus 로고    scopus 로고
    • Adsorption of fibrinogen on tantalum oxide, titanium oxide and gold studied by the QCM-D technique
    • Hemmersam A.G., Foss M., Chevallier J., and Besenbacher F. Adsorption of fibrinogen on tantalum oxide, titanium oxide and gold studied by the QCM-D technique. Colloids Surf B Biointerfaces 43 (2005) 208-215
    • (2005) Colloids Surf B Biointerfaces , vol.43 , pp. 208-215
    • Hemmersam, A.G.1    Foss, M.2    Chevallier, J.3    Besenbacher, F.4
  • 40
    • 0037635409 scopus 로고    scopus 로고
    • Functional incorporation of integrins into solid supported membranes on ultrathin films of cellulose: impact on adhesion
    • 'Blood platelet integrin receptors alpha(IIb)beta(3) were reconstituted into vesicles which were then spread either on ultrathin films of cellulose or on bare glass. The functionality of receptors on both supports was compared by measuring their adhesion strength to giant vesicles. The adhesion energy of integrins on glass was much lower compared to cellulose supported integrins.'
    • Goennenwein S., Tanaka M., Hu B., Moroder L., and Sackmann E. Functional incorporation of integrins into solid supported membranes on ultrathin films of cellulose: impact on adhesion. Biophys J 85 (2003) 646-655. 'Blood platelet integrin receptors alpha(IIb)beta(3) were reconstituted into vesicles which were then spread either on ultrathin films of cellulose or on bare glass. The functionality of receptors on both supports was compared by measuring their adhesion strength to giant vesicles. The adhesion energy of integrins on glass was much lower compared to cellulose supported integrins.'
    • (2003) Biophys J , vol.85 , pp. 646-655
    • Goennenwein, S.1    Tanaka, M.2    Hu, B.3    Moroder, L.4    Sackmann, E.5
  • 41
    • 4644266072 scopus 로고    scopus 로고
    • Incorporation of integrins into artificial planar lipid membranes: characterization by plasmon-enhanced fluorescence spectroscopy
    • 1 of the integrin superfamily were inserted into artificial planar bilayers and were characterized by surface plasmon-enhanced fluorescence spectroscopy. The function of the integrins could be maintained by their incorporation into peptide tethered lipid membranes.'
    • 1 of the integrin superfamily were inserted into artificial planar bilayers and were characterized by surface plasmon-enhanced fluorescence spectroscopy. The function of the integrins could be maintained by their incorporation into peptide tethered lipid membranes.'
    • (2004) Anal Biochem , vol.333 , pp. 216-224
    • Sinner, E.K.1    Reuning, U.2    Kok, F.N.3    Sacca, B.4    Moroder, L.5    Knoll, W.6
  • 42
    • 33744802398 scopus 로고    scopus 로고
    • Effects of surface tethering on protein folding mechanisms
    • 'Depending at which polypeptide position a protein is tethered to a supporting surface its folding mechanism is altered. Tethering to structured and to unstructured regions is preferred over that to partially structured regions.'
    • Friedel M., Baumketner A., and Shea J.E. Effects of surface tethering on protein folding mechanisms. Proc Natl Acad Sci U S A 103 (2006) 8396-8401. 'Depending at which polypeptide position a protein is tethered to a supporting surface its folding mechanism is altered. Tethering to structured and to unstructured regions is preferred over that to partially structured regions.'
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8396-8401
    • Friedel, M.1    Baumketner, A.2    Shea, J.E.3
  • 43
    • 33751225988 scopus 로고    scopus 로고
    • High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer
    • Milhiet P.E., Gubellini F., Berquand A., Dosset P., Rigaud J.L., Le Grimellec C., et al. High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer. Biophys J 91 (2006) 3268-3275
    • (2006) Biophys J , vol.91 , pp. 3268-3275
    • Milhiet, P.E.1    Gubellini, F.2    Berquand, A.3    Dosset, P.4    Rigaud, J.L.5    Le Grimellec, C.6
  • 44
    • 0036629043 scopus 로고    scopus 로고
    • Membrane proteins: functional and structural studies using reconstituted proteoliposomes and 2-D crystals
    • Rigaud J.L. Membrane proteins: functional and structural studies using reconstituted proteoliposomes and 2-D crystals. Braz J Med Biol Res 35 (2002) 753-766
    • (2002) Braz J Med Biol Res , vol.35 , pp. 753-766
    • Rigaud, J.L.1
  • 45
    • 0242573084 scopus 로고    scopus 로고
    • Membrane protein reconstitution and crystallization by controlled dilution
    • Remigy H.W., Caujolle-Bert D., Suda K., Schenk A., Chami M., and Engel A. Membrane protein reconstitution and crystallization by controlled dilution. FEBS Lett 555 (2003) 160-169
    • (2003) FEBS Lett , vol.555 , pp. 160-169
    • Remigy, H.W.1    Caujolle-Bert, D.2    Suda, K.3    Schenk, A.4    Chami, M.5    Engel, A.6
  • 46
    • 0035608351 scopus 로고    scopus 로고
    • Functional tethered membranes
    • Sinner E.K., and Knoll W. Functional tethered membranes. Curr Opin Chem Biol 5 (2001) 705-711
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 705-711
    • Sinner, E.K.1    Knoll, W.2
  • 47
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer P., and Dufrene Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat Methods 3 (2006) 347-355
    • (2006) Nat Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 48
    • 27944496013 scopus 로고    scopus 로고
    • Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy
    • 'Development of a protocol to attach any given O6-alkylguanine-DNA-alkyltransferase (hAGT) fused protein selectively and covalently to gold and glass surfaces for their further characterization by SMFS.'
    • Kufer S.K., Dietz H., Albrecht C., Blank K., Kardinal A., Rief M., et al. Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy. Eur Biophys J 35 (2005) 72-78. 'Development of a protocol to attach any given O6-alkylguanine-DNA-alkyltransferase (hAGT) fused protein selectively and covalently to gold and glass surfaces for their further characterization by SMFS.'
    • (2005) Eur Biophys J , vol.35 , pp. 72-78
    • Kufer, S.K.1    Dietz, H.2    Albrecht, C.3    Blank, K.4    Kardinal, A.5    Rief, M.6
  • 49
    • 4644305444 scopus 로고    scopus 로고
    • Controlled immobilization of membrane proteins to surfaces for fourier transform infrared investigations
    • 'Hexahistidine sequences present in the membrane protein or lipid bilayer are used to immobilize membrane proteins uniformly and reversibly onto a supporting surface. Fourier transform infrared spectroscopy is used to screen the function of cellular receptors reversibly immobilized by the approach.'
    • Rigler P., Ulrich W.P., and Vogel H. Controlled immobilization of membrane proteins to surfaces for fourier transform infrared investigations. Langmuir 20 (2004) 7901-7903. 'Hexahistidine sequences present in the membrane protein or lipid bilayer are used to immobilize membrane proteins uniformly and reversibly onto a supporting surface. Fourier transform infrared spectroscopy is used to screen the function of cellular receptors reversibly immobilized by the approach.'
    • (2004) Langmuir , vol.20 , pp. 7901-7903
    • Rigler, P.1    Ulrich, W.P.2    Vogel, H.3
  • 50
    • 24744472221 scopus 로고    scopus 로고
    • High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies
    • 'The authors present multivalent metal-chelating thiols suitable to bind histidine-tagged proteins. The thiols can be used to coat a supporting surface and to immobilize histidine-tagged proteins uniformly and oriented. Proteins tagged retain their functionality.'
    • Tinazli A., Tang J., Valiokas R., Picuric S., Lata S., Piehler J., et al. High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies. Chemistry 11 (2005) 5249-5259. 'The authors present multivalent metal-chelating thiols suitable to bind histidine-tagged proteins. The thiols can be used to coat a supporting surface and to immobilize histidine-tagged proteins uniformly and oriented. Proteins tagged retain their functionality.'
    • (2005) Chemistry , vol.11 , pp. 5249-5259
    • Tinazli, A.1    Tang, J.2    Valiokas, R.3    Picuric, S.4    Lata, S.5    Piehler, J.6
  • 51
    • 0033635139 scopus 로고    scopus 로고
    • Design of supported membranes tethered via metal-affinity ligand-receptor pairs
    • Radler U., Mack J., Persike N., Jung G., and Tampe R. Design of supported membranes tethered via metal-affinity ligand-receptor pairs. Biophys J 79 (2000) 3144-3152
    • (2000) Biophys J , vol.79 , pp. 3144-3152
    • Radler, U.1    Mack, J.2    Persike, N.3    Jung, G.4    Tampe, R.5
  • 52
    • 10344264935 scopus 로고    scopus 로고
    • The protein-tethered lipid bilayer: a novel mimic of the biological membrane
    • Giess F., Friedrich M.G., Heberle J., Naumann R.L., and Knoll W. The protein-tethered lipid bilayer: a novel mimic of the biological membrane. Biophys J 87 (2004) 3213-3220
    • (2004) Biophys J , vol.87 , pp. 3213-3220
    • Giess, F.1    Friedrich, M.G.2    Heberle, J.3    Naumann, R.L.4    Knoll, W.5
  • 53
    • 33746238085 scopus 로고    scopus 로고
    • An approach to prepare membrane proteins for single-molecule imaging
    • 'After engineering a cysteine residue into an aqueous loop, solubilized porin OmpF could be covalently attached to ultraflat gold surfaces. After this, detergent/lipid micelles were added to reconstitute the protein into the hydrophobic lipid chains. AFM topographs show the unidirectional orientation of the membrane proteins.'
    • Cisneros D.A., Muller D.J., Daud S.M., and Lakey J.H. An approach to prepare membrane proteins for single-molecule imaging. Angew Chem [Int Ed Engl] 45 (2006) 3252-3256. 'After engineering a cysteine residue into an aqueous loop, solubilized porin OmpF could be covalently attached to ultraflat gold surfaces. After this, detergent/lipid micelles were added to reconstitute the protein into the hydrophobic lipid chains. AFM topographs show the unidirectional orientation of the membrane proteins.'
    • (2006) Angew Chem [Int Ed Engl] , vol.45 , pp. 3252-3256
    • Cisneros, D.A.1    Muller, D.J.2    Daud, S.M.3    Lakey, J.H.4
  • 54
    • 0032560496 scopus 로고    scopus 로고
    • Immobilization strategies for biological scanning probe microscopy
    • Wagner P. Immobilization strategies for biological scanning probe microscopy. FEBS Lett. 430 (1998) 112-115
    • (1998) FEBS Lett. , vol.430 , pp. 112-115
    • Wagner, P.1
  • 55
  • 56
    • 0037434143 scopus 로고    scopus 로고
    • Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces
    • Schiller S.M., Naumann R., Lovejoy K., Kunz H., and Knoll W. Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces. Angew Chem Int Ed Engl 42 (2003) 208-211
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 208-211
    • Schiller, S.M.1    Naumann, R.2    Lovejoy, K.3    Kunz, H.4    Knoll, W.5
  • 57
    • 29444456640 scopus 로고    scopus 로고
    • Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule. 1. Incorporation of channel peptides
    • He L., Robertson J.W., Li J., Karcher I., Schiller S.M., Knoll W., et al. Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule. 1. Incorporation of channel peptides. Langmuir 21 (2005) 11666-11672
    • (2005) Langmuir , vol.21 , pp. 11666-11672
    • He, L.1    Robertson, J.W.2    Li, J.3    Karcher, I.4    Schiller, S.M.5    Knoll, W.6
  • 58
    • 2442551468 scopus 로고    scopus 로고
    • Supported membranes with well-defined polymer tethers-incorporation of cell receptors
    • 3) could be incorporated into the polymer-tethered membrane.'
    • 3) could be incorporated into the polymer-tethered membrane.'
    • (2004) Chemphyschem , vol.5 , pp. 327-335
    • Purrucker, O.1    Fortig, A.2    Jordan, R.3    Tanaka, M.4
  • 59
    • 0042285088 scopus 로고    scopus 로고
    • Fabrication of solid-state nanopores with single-nanometre precision
    • Storm A.J., Chen J.H., Ling X.S., Zandbergen H.W., and Dekker C. Fabrication of solid-state nanopores with single-nanometre precision. Nat Mater 2 (2003) 537-540
    • (2003) Nat Mater , vol.2 , pp. 537-540
    • Storm, A.J.1    Chen, J.H.2    Ling, X.S.3    Zandbergen, H.W.4    Dekker, C.5
  • 60
    • 30344455631 scopus 로고    scopus 로고
    • Cell membranes suspended across nanoaperture arrays
    • 4 support. Both extracellular and intracellular surfaces of these cell membranes could be targeted using side-specific fluorescent markers. The approach is of interest for studying ligand-receptor interactions at the single-molecule level using optical, electrical, and scanning probe techniques.'
    • 4 support. Both extracellular and intracellular surfaces of these cell membranes could be targeted using side-specific fluorescent markers. The approach is of interest for studying ligand-receptor interactions at the single-molecule level using optical, electrical, and scanning probe techniques.'
    • (2006) Langmuir , vol.22 , pp. 22-25
    • Danelon, C.1    Perez, J.B.2    Santschi, C.3    Brugger, J.4    Vogel, H.5
  • 61
    • 33751206244 scopus 로고    scopus 로고
    • Two-chamber AFM: probing membrane proteins separating two aqueous compartments
    • 'For the first time AFM has been applied to image protein membranes freely spanning over nanometer sized holes. The spatial resolution achieved is sufficient to resolve the crystal lattice of the bacterial S-layer. After covering the holes by purple membrane it was possible to activate the light-driven proton pumps residing in the membrane and to induce a pH gradient..
    • Goncalves R.P., Agnus G., Sens P., Houssin C., Bartenlian B., and Scheuring S. Two-chamber AFM: probing membrane proteins separating two aqueous compartments. Nat Methods 3 (2006) 1007-1012. 'For the first time AFM has been applied to image protein membranes freely spanning over nanometer sized holes. The spatial resolution achieved is sufficient to resolve the crystal lattice of the bacterial S-layer. After covering the holes by purple membrane it was possible to activate the light-driven proton pumps residing in the membrane and to induce a pH gradient..
    • (2006) Nat Methods , vol.3 , pp. 1007-1012
    • Goncalves, R.P.1    Agnus, G.2    Sens, P.3    Houssin, C.4    Bartenlian, B.5    Scheuring, S.6
  • 62
    • 33846006521 scopus 로고    scopus 로고
    • S-layers as a basic building block in a molecular construction kit
    • Sleytr U.B., Egelseer E.M., Ilk N., Pum D., and Schuster B. S-layers as a basic building block in a molecular construction kit. Febs J 274 (2007) 323-334
    • (2007) Febs J , vol.274 , pp. 323-334
    • Sleytr, U.B.1    Egelseer, E.M.2    Ilk, N.3    Pum, D.4    Schuster, B.5
  • 63
    • 23744506838 scopus 로고    scopus 로고
    • Locating ligand binding and activation of a single antiporter
    • 'This paper shows for the first time that SMFS can detect interactions occurring upon activating a transmembrane protein. The binding of a single ligand being as small as a sodium ion could be detected and located on the three-dimensional structure of the sodium/proton driven antiporter NhaA from E. coli.'
    • Kedrov A., Krieg M., Ziegler C., Kuhlbrandt W., and Muller D.J. Locating ligand binding and activation of a single antiporter. EMBO Rep 6 (2005) 668-674. 'This paper shows for the first time that SMFS can detect interactions occurring upon activating a transmembrane protein. The binding of a single ligand being as small as a sodium ion could be detected and located on the three-dimensional structure of the sodium/proton driven antiporter NhaA from E. coli.'
    • (2005) EMBO Rep , vol.6 , pp. 668-674
    • Kedrov, A.1    Krieg, M.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 64
    • 34249676251 scopus 로고    scopus 로고
    • Stabilizing effect of Zn2+ in native bovine rhodopsin
    • 2+ on the interactions stabilizing bovine rhodopsin. SMFS assays revealed the strength and location of interactions that stabilize structural segments within this receptor. The possibility to characterize the stability of a receptor in dependence of physiological relevant environmental conditions is medically and biotechnologically important.'
    • 2+ on the interactions stabilizing bovine rhodopsin. SMFS assays revealed the strength and location of interactions that stabilize structural segments within this receptor. The possibility to characterize the stability of a receptor in dependence of physiological relevant environmental conditions is medically and biotechnologically important.'
    • (2007) J Biol Chem , vol.282 , pp. 11377-11385
    • Park, P.S.1    Sapra, K.T.2    Kolinski, M.3    Filipek, S.4    Palczewski, K.5    Muller, D.J.6
  • 65
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • 'AFM topographs show water-soluble toxins secreted from bacteria inserting into a supported lipid bilayer. Time-lapse AFM follows perfringolysin O (PFO) assembling into a prepore that vertically collapses onto the membrane forming the toxic pore.'
    • Czajkowsky D.M., Hotze E.M., Shao Z., and Tweten R.K. Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. EMBO J 23 (2004) 3206-3215. 'AFM topographs show water-soluble toxins secreted from bacteria inserting into a supported lipid bilayer. Time-lapse AFM follows perfringolysin O (PFO) assembling into a prepore that vertically collapses onto the membrane forming the toxic pore.'
    • (2004) EMBO J , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.