메뉴 건너뛰기




Volumn 16, Issue 4, 2006, Pages 489-495

Single-molecule studies of membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MEMBRANE PROTEIN; OLIGOMER;

EID: 33746606443     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.06.001     Document Type: Review
Times cited : (88)

References (43)
  • 1
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the atomic force microscope
    • Müller D.J., Fotiadis D., and Engel A. Mapping flexible protein domains at subnanometer resolution with the atomic force microscope. FEBS Lett 430 (1998) 105-111
    • (1998) FEBS Lett , vol.430 , pp. 105-111
    • Müller, D.J.1    Fotiadis, D.2    Engel, A.3
  • 2
    • 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
  • 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
    • 0033861876 scopus 로고    scopus 로고
    • Model energy landscapes and the force-induced dissociation of ligand-receptor bonds
    • Strunz T., Oroszlan K., Schumakovitch I., Guntherodt H., and Hegner M. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys J 79 (2000) 1206-1212
    • (2000) Biophys J , vol.79 , pp. 1206-1212
    • Strunz, T.1    Oroszlan, K.2    Schumakovitch, I.3    Guntherodt, H.4    Hegner, M.5
  • 6
  • 7
    • 0036195902 scopus 로고    scopus 로고
    • Imaging the electrostatic potential of transmembrane channels: atomic probe microscopy on OmpF porin
    • Philippsen A., Im W., Engel A., Schirmer T., Roux B., and Müller D.J. Imaging the electrostatic potential of transmembrane channels: atomic probe microscopy on OmpF porin. Biophys J 82 (2002) 1667-1676
    • (2002) Biophys J , vol.82 , pp. 1667-1676
    • Philippsen, A.1    Im, W.2    Engel, A.3    Schirmer, T.4    Roux, B.5    Müller, D.J.6
  • 8
    • 21144452622 scopus 로고    scopus 로고
    • Assessment of insulated conductive cantilevers for biology and electrochemistry
    • Development of a conducting AFM probe for the characterization of membrane proteins.
    • Frederix P.L.T.M., Gullo M.R., Akiyama T., Tonin A., de Rooij N.F., Staufer U., and Engel A. Assessment of insulated conductive cantilevers for biology and electrochemistry. Nanotechnology 16 (2005) 997-1005. Development of a conducting AFM probe for the characterization of membrane proteins.
    • (2005) Nanotechnology , vol.16 , pp. 997-1005
    • Frederix, P.L.T.M.1    Gullo, M.R.2    Akiyama, T.3    Tonin, A.4    de Rooij, N.F.5    Staufer, U.6    Engel, A.7
  • 9
    • 17844392351 scopus 로고    scopus 로고
    • Structural biology. Nature's rotary electromotors
    • Junge W., and Nelson N. Structural biology. Nature's rotary electromotors. Science 308 (2005) 642-644
    • (2005) Science , vol.308 , pp. 642-644
    • Junge, W.1    Nelson, N.2
  • 10
    • 0345096520 scopus 로고    scopus 로고
    • Electrical power fuels rotary ATP synthase
    • Dimroth P., von Ballmoos C., Meier T., and Kaim G. Electrical power fuels rotary ATP synthase. Structure 11 (2003) 1469-1473
    • (2003) Structure , vol.11 , pp. 1469-1473
    • Dimroth, P.1    von Ballmoos, C.2    Meier, T.3    Kaim, G.4
  • 14
    • 0032568640 scopus 로고    scopus 로고
    • Architecture and mechanism of the light-harvesting apparatus of purple bacteria
    • Hu X., Damjanovic A., Ritz T., and Schulten K. Architecture and mechanism of the light-harvesting apparatus of purple bacteria. Proc Natl Acad Sci USA 95 (1998) 5935-5941
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5935-5941
    • Hu, X.1    Damjanovic, A.2    Ritz, T.3    Schulten, K.4
  • 15
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM
    • Scheuring S., Seguin J., Marco S., Levy D., Robert B., and Rigaud J.L. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM. Proc Natl Acad Sci USA 100 (2003) 1690-1693
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Levy, D.4    Robert, B.5    Rigaud, J.L.6
  • 16
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • The structural rearrangement in response to light of photosynthetic membranes of a bacterium was investigated. The observed structural adaptation ensures efficient photon capture under low-light conditions and prevents photodamage under high-light conditions.
    • Scheuring S., and Sturgis J.N. Chromatic adaptation of photosynthetic membranes. Science 309 (2005) 484-487. The structural rearrangement in response to light of photosynthetic membranes of a bacterium was investigated. The observed structural adaptation ensures efficient photon capture under low-light conditions and prevents photodamage under high-light conditions.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 17
    • 4344704617 scopus 로고    scopus 로고
    • The native architecture of a photosynthetic membrane
    • This first view of any multicomponent membrane shows the relative positions and associations of the photosynthetic complexes and reveals new features of the network organization.
    • Bahatyrova S., Frese R.N., Siebert C.A., Olsen J.D., Van Der Werf K.O., Van Grondelle R., Niederman R.A., Bullough P.A., Otto C., and Hunter C.N. The native architecture of a photosynthetic membrane. Nature 430 (2004) 1058-1062. This first view of any multicomponent membrane shows the relative positions and associations of the photosynthetic complexes and reveals new features of the network organization.
    • (2004) Nature , vol.430 , pp. 1058-1062
    • Bahatyrova, S.1    Frese, R.N.2    Siebert, C.A.3    Olsen, J.D.4    Van Der Werf, K.O.5    Van Grondelle, R.6    Niederman, R.A.7    Bullough, P.A.8    Otto, C.9    Hunter, C.N.10
  • 18
    • 12544254339 scopus 로고    scopus 로고
    • Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy
    • Scheuring S., Busselez J., and Levy D. Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy. J Biol Chem 280 (2005) 1426-1431
    • (2005) J Biol Chem , vol.280 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Levy, D.3
  • 19
    • 11144246948 scopus 로고    scopus 로고
    • Membrane insertion of Rhodopseudomonas acidophila light harvesting complex 2 investigated by high resolution AFM
    • Goncalves R.P., Busselez J., Levy D., Seguin J., and Scheuring S. Membrane insertion of Rhodopseudomonas acidophila light harvesting complex 2 investigated by high resolution AFM. J Struct Biol 149 (2005) 79-86
    • (2005) J Struct Biol , vol.149 , pp. 79-86
    • Goncalves, R.P.1    Busselez, J.2    Levy, D.3    Seguin, J.4    Scheuring, S.5
  • 20
    • 33645100807 scopus 로고    scopus 로고
    • The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization
    • Scheuring S., Goncalves R.P., Prima V., and Sturgis J.N. The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization. J Mol Biol 358 (2006) 83-96
    • (2006) J Mol Biol , vol.358 , pp. 83-96
    • Scheuring, S.1    Goncalves, R.P.2    Prima, V.3    Sturgis, J.N.4
  • 21
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: rhodopsin dimers in native disc membranes
    • In this work the native arrangement of Rho is demonstrated for the first time by AFM of disk membranes.
    • 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. In this work the native arrangement of Rho is demonstrated for the first time by AFM of disk membranes.
    • (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
  • 23
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y., Fotiadis D., Filipek S., Saperstein D.A., Palczewski K., and Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J Biol Chem 278 (2003) 21655-21662
    • (2003) J Biol Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 25
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation
    • Guo W., Shi L., Filizola M., Weinstein H., and Javitch J.A. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc Natl Acad Sci USA 102 (2005) 17495-17500
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 26
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros J.A., Shi L., and Javitch J.A. Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 60 (2001) 1-19
    • (2001) Mol Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 28
    • 33645097568 scopus 로고    scopus 로고
    • Detecting molecular interactions that stabilize bovine rhodopsin
    • Molecular interactions that establish stable structural segments within Rho are detected by SMFS. These segments harbor highly conserved residues (>80%), which ensure the stability of Rho.
    • Sapra K.T., Park P.S.-H., Filipek S., Engel A., Palczewski K., and Müller D.J. Detecting molecular interactions that stabilize bovine rhodopsin. J Mol Biol 358 (2006) 255-269. Molecular interactions that establish stable structural segments within Rho are detected by SMFS. These segments harbor highly conserved residues (>80%), which ensure the stability of Rho.
    • (2006) J Mol Biol , vol.358 , pp. 255-269
    • Sapra, K.T.1    Park, P.S.-H.2    Filipek, S.3    Engel, A.4    Palczewski, K.5    Müller, D.J.6
  • 29
    • 0029088343 scopus 로고
    • Molecular genetics of Retinitis pigmentosa
    • Dryja T.P., and Li T. Molecular genetics of Retinitis pigmentosa. Hum Mol Genet 4 (1995) 1739-1743
    • (1995) Hum Mol Genet , vol.4 , pp. 1739-1743
    • Dryja, T.P.1    Li, T.2
  • 30
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov A., Ziegler C., Janovjak H., Kühlbrandt W., and Müller D.J. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J Mol Biol 340 (2004) 1143-1152
    • (2004) J Mol Biol , vol.340 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kühlbrandt, W.4    Müller, D.J.5
  • 31
    • 33644844356 scopus 로고    scopus 로고
    • Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM
    • Kessler M., and Gaub H.E. Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM. Structure 14 (2006) 521-527
    • (2006) Structure , vol.14 , pp. 521-527
    • Kessler, M.1    Gaub, H.E.2
  • 32
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros D.A., Oesterhelt D., and Muller D.J. Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure 13 (2005) 235-242
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 33
    • 33645124465 scopus 로고    scopus 로고
    • Characterizing folding, structure, molecular interactions and ligand gated activation of single sodium/proton antiporters
    • Kedrov A., and Müller D.J. Characterizing folding, structure, molecular interactions and ligand gated activation of single sodium/proton antiporters. Naunyn Schmiedebergs Arch Pharmacol 372 (2006) 400-412
    • (2006) Naunyn Schmiedebergs Arch Pharmacol , vol.372 , pp. 400-412
    • Kedrov, A.1    Müller, D.J.2
  • 35
    • 23744506838 scopus 로고    scopus 로고
    • Locating ligand binding and activation of a single antiporter
    • +) could be localized. Statistical analysis of single molecule events revealed insights into underlying activation mechanisms.
    • +) could be localized. Statistical analysis of single molecule events revealed insights into underlying activation mechanisms.
    • (2005) EMBO Rep , vol.6 , pp. 668-674
    • Kedrov, A.1    Krieg, M.2    Ziegler, C.3    Kuhlbrandt, W.4    Müller, D.J.5
  • 37
    • 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
  • 38
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • Time-lapse AFM shows a change in height of pore-forming cholesterol-dependent cytolysins. The prepore protrudes from the membrane surface by ∼11.3 nm and by 7.3 nm from the 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. Time-lapse AFM shows a change in height of pore-forming cholesterol-dependent cytolysins. The prepore protrudes from the membrane surface by ∼11.3 nm and by 7.3 nm from the pore.
    • (2004) EMBO J , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 39
    • 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
    • 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
    • (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
  • 40
    • 9144264281 scopus 로고    scopus 로고
    • Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum
    • Scheuring S., Rigaud J.L., and Sturgis J.N. Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum. EMBO J 23 (2004) 4127-4133
    • (2004) EMBO J , vol.23 , pp. 4127-4133
    • Scheuring, S.1    Rigaud, J.L.2    Sturgis, J.N.3
  • 41
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., and Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276 (1997) 1109-1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 43
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: new insights from structural and biochemical studies
    • Okada T., Ernst O.P., Palczewski K., and Hofmann K.P. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem Sci 26 (2001) 318-324
    • (2001) Trends Biochem Sci , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.