메뉴 건너뛰기




Volumn 2002, Issue 68, 2002, Pages 257-299

Conformations, flexibility, and interactions observed on individual membrane proteins by atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BACTERIAL PROTEIN; MEMBRANE PROTEIN; PROTEIN SUBUNIT;

EID: 0036362081     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(02)68014-8     Document Type: Review
Times cited : (18)

References (154)
  • 2
    • 0017283996 scopus 로고
    • Evidence for chromophore-chromophore interactions in the purple membrane from reconstitution experiments of the chromophore-free membrane
    • Bauer, P.-J., Dencher, N. A., and Heyn, M. P. (1976). Evidence for chromophore-chromophore interactions in the purple membrane from reconstitution experiments of the chromophore-free membrane. Biophys. Struct. Mech. 2, 79-92.
    • (1976) Biophys. Struct. Mech. , vol.2 , pp. 79-92
    • Bauer, P.-J.1    Dencher, N.A.2    Heyn, M.P.3
  • 3
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans
    • Baumeister, W., Barth, M., Hegerl, R., Guckenberger, R., Hahn, M., and Saxton, W. O. (1986). Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans. J. Mol. Biol. 187, 241-253.
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 4
    • 0022504356 scopus 로고
    • Can S-layers make bacterial connexons?
    • Baumeister, W., and Hegerl, R. (1986). Can S-layers make bacterial connexons? FEMS Microbiol. Lett. 36, 119-125.
    • (1986) FEMS Microbiol. Lett. , vol.36 , pp. 119-125
    • Baumeister, W.1    Hegerl, R.2
  • 5
    • 0023953848 scopus 로고
    • Bacterial surface proteins: Some structural, functional and evolutionary aspects
    • Baumeister, W., Wildhaber, I., and Engelhardt, H. (1988). Bacterial surface proteins: Some structural, functional and evolutionary aspects. Biophys. Chem. 29, 39-49.
    • (1988) Biophys. Chem. , vol.29 , pp. 39-49
    • Baumeister, W.1    Wildhaber, I.2    Engelhardt, H.3
  • 6
    • 0017648436 scopus 로고
    • Effects of bleaching and regeneration on the purple membrane structure of Halobacterium halobium
    • Becher, B., and Cassim, J. Y. (1977). Effects of bleaching and regeneration on the purple membrane structure of Halobacterium halobium. Biophys. J. 19, 285-297.
    • (1977) Biophys. J. , vol.19 , pp. 285-297
    • Becher, B.1    Cassim, J.Y.2
  • 7
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 a resolution
    • Belrhali, H., Nollert, P., Royant, A., Menzel, C., Rosenbusch, J. P., Landau, E. M., and Pebay-Peyroula, E. (1999). Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution. Struct. Fold. Des. 7, 909-917.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 11
    • 0022799046 scopus 로고
    • Reconstitution of molecule images analysed by correspondence analysis: A tool for structural interpretation
    • Bretaudiere, J.-P., and Frank, J. (1986). Reconstitution of molecule images analysed by correspondence analysis: a tool for structural interpretation. J. Microsc. 144, 1-14.
    • (1986) J. Microsc. , vol.144 , pp. 1-14
    • Bretaudiere, J.-P.1    Frank, J.2
  • 12
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A., and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 13
    • 0026317248 scopus 로고
    • Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope
    • Butt, H.-J. (1991). Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope. Biophys. J. 60, 1438-1444.
    • (1991) Biophys. J. , vol.60 , pp. 1438-1444
    • Butt, H.-J.1
  • 14
    • 0026657705 scopus 로고
    • Measuring local surface charge densities in electrolyte solutions with a scanning force microscope
    • Butt, H.-J. (1992). Measuring local surface charge densities in electrolyte solutions with a scanning force microscope. Biophys. J. 63, 578-582.
    • (1992) Biophys. J. , vol.63 , pp. 578-582
    • Butt, H.-J.1
  • 15
    • 11744267490 scopus 로고
    • Measuring surface forces in aqueous solution with the atomic force microscope
    • Butt, H.-J., Jaschke, M., and Ducker, W. (1995). Measuring surface forces in aqueous solution with the atomic force microscope. Bioelect. Bioenerg. 38, 191-201.
    • (1995) Bioelect. Bioenerg. , vol.38 , pp. 191-201
    • Butt, H.-J.1    Jaschke, M.2    Ducker, W.3
  • 17
    • 0001138858 scopus 로고    scopus 로고
    • Carbon nanotube atomic force microscopy tips: Direct growth by chemical vapor deposition and application to high-resolution imaging
    • Cheung, C. L., Hafner, J. H., and Lieber, C. M. (2000). Carbon nanotube atomic force microscopy tips: direct growth by chemical vapor deposition and application to high-resolution imaging. Proc. Natl. Acad. Sci. U.S.A. 97, 3809-3813.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3809-3813
    • Cheung, C.L.1    Hafner, J.H.2    Lieber, C.M.3
  • 19
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal α-Hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., Sheng, S., and Shao, Z. (1998). Staphylococcal α-Hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276, 325-330.
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 21
    • 0028949325 scopus 로고
    • Binding strength between cell adhesion proteoglycans measured by atomic force microscopy
    • Dammer, U., Popescu, O., Wagner, P., Anselmetti, D., Güntherodt, H. J., and Misevic, G. N. (1995). Binding strength between cell adhesion proteoglycans measured by atomic force microscopy. Science 267, 1173-1175.
    • (1995) Science , vol.267 , pp. 1173-1175
    • Dammer, U.1    Popescu, O.2    Wagner, P.3    Anselmetti, D.4    Güntherodt, H.J.5    Misevic, G.N.6
  • 22
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: Insights from electrophysiology
    • Delcour, A. (1997). Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol. Lett. 151, 115-123.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 115-123
    • Delcour, A.1
  • 23
    • 0026691772 scopus 로고
    • Membrane-derived oligosaccharides (MDOs) promote closing of an E. coli channel
    • Delcour, A. H., Adler, J., Kung, C., and Martinac, B. (1992). Membrane-derived oligosaccharides (MDOs) promote closing of an E. coli channel. FEBS Lett. 304, 216-220.
    • (1992) FEBS Lett. , vol.304 , pp. 216-220
    • Delcour, A.H.1    Adler, J.2    Kung, C.3    Martinac, B.4
  • 24
    • 0028828533 scopus 로고
    • Cadaverine induces closing of E. coli porins
    • dela Vega, A. L., and Delcour, A. H. (1995). Cadaverine induces closing of E. coli porins. EMBO J. 14, 6058-6065.
    • (1995) EMBO J. , vol.14 , pp. 6058-6065
    • Dela Vega, A.L.1    Delcour, A.H.2
  • 25
    • 0024744871 scopus 로고
    • Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
    • Dencher, N. A., Dresselhaus, D., Zaccai, G., and Büldt, G. (1989). Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl. Acad. Sci. U.S.A. 86, 7876-7879.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Büldt, G.4
  • 26
    • 0033529291 scopus 로고    scopus 로고
    • o ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme
    • o ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme. Proc. Natl. Acad. Sci. U.S.A. 96, 7785-7790.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7785-7790
    • Dmitriev, O.Y.1    Jones, P.C.2    Fillingame, R.H.3
  • 29
    • 0030757526 scopus 로고    scopus 로고
    • Nanoscopic structure of DNA condensed for gene delivery
    • Dunlap, D. D., Maggi, A., Soria, M. R., and Monaco, L. (1997). Nanoscopic structure of DNA condensed for gene delivery. Nucl. Acids Res. 25, 3095.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3095
    • Dunlap, D.D.1    Maggi, A.2    Soria, M.R.3    Monaco, L.4
  • 31
    • 0020158294 scopus 로고
    • Mass mapping of a protein complex with the scanning transmission electron microscope
    • Engel, A., Baumeister, W., and Saxton, W. (1982). Mass mapping of a protein complex with the scanning transmission electron microscope. Proc. Natl. Acad. Sci. U.S.A. 79, 4050-4054.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4050-4054
    • Engel, A.1    Baumeister, W.2    Saxton, W.3
  • 32
    • 0033084066 scopus 로고    scopus 로고
    • Atomic force microscopy: A powerful tool to observe biomolecules at work
    • Engel, A., Lyubchenko, Y., and Müller, D. J. (1999). Atomic force microscopy: A powerful tool to observe biomolecules at work. Trends Cell Biol. 9, 77-80.
    • (1999) Trends Cell Biol. , vol.9 , pp. 77-80
    • Engel, A.1    Lyubchenko, Y.2    Müller, D.J.3
  • 33
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L.-O., Siegert, R., Lehmann, W. D., and Oesterhelt, D. (1998). Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. U.S.A. 95, 11,673-11,678.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95
    • Essen, L.-O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 35
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.-L., Moy, V. T., and Gaub, H. E. (1994). Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 36
    • 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. (2000). Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J. Mol. Biol. 300, 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
  • 38
    • 84985224954 scopus 로고
    • Classification of images of biomolecular assemblies: A study of ribosomes and ribosomal subunits of Escheria coli
    • Frank, J., Bretaudiere, J.-P., Carazo, J.-M., Veschoor, A., and Wagenknecht, T. (1987). Classification of images of biomolecular assemblies: A study of ribosomes and ribosomal subunits of Escheria coli. J. Microsc. 150, 99-115.
    • (1987) J. Microsc. , vol.150 , pp. 99-115
    • Frank, J.1    Bretaudiere, J.-P.2    Carazo, J.-M.3    Veschoor, A.4    Wagenknecht, T.5
  • 40
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J. E., Braha, O., Hobaugh, M. R., Song, L., Cheley, S., Shustak, C., and Bayley, H. (1994). Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. U.S.A. 91, 12828-31.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 41
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M., and Henderson, R. (1996). Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 42
    • 0030845490 scopus 로고    scopus 로고
    • Model of the c-subunit oligomer in the membrane domain of F-ATPases
    • Groth, G., and Walker, J. E. (1997). Model of the c-subunit oligomer in the membrane domain of F-ATPases. FEBS Lett. 410, 117-123.
    • (1997) FEBS Lett. , vol.410 , pp. 117-123
    • Groth, G.1    Walker, J.E.2
  • 43
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • Gu, L. Q., Braha, O., Conlan, S., Cheley, S., and Bayley, H. (1999). Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter [see comments]. Nature 398(6729), 686-690.
    • (1999) Nature , vol.398 , Issue.6729 , pp. 686-690
    • Gu, L.Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 45
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and Freire, E. (1995). Forces and factors that contribute to the structural stability of membrane proteins. BBA-Bioenerg. 1228, 1-27.
    • (1995) BBA-Bioenerg. , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 49
    • 0033121032 scopus 로고    scopus 로고
    • Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope
    • Heinz, W. F., and Hoh, J. H. (1999). Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope. Nanotechnology 17, 143-150.
    • (1999) Nanotechnology , vol.17 , pp. 143-150
    • Heinz, W.F.1    Hoh, J.H.2
  • 50
    • 0030606017 scopus 로고    scopus 로고
    • Structure and function of proteins in G-protein coupled signal transfer
    • Helmreich, E. J. M., and Hofmann, K.-P. (1996). Structure and function of proteins in G-protein coupled signal transfer. Biochem. Biophys. Acta 1286, 285-322.
    • (1996) Biochem. Biophys. Acta , vol.1286 , pp. 285-322
    • Helmreich, E.J.M.1    Hofmann, K.-P.2
  • 53
  • 54
    • 0027163746 scopus 로고
    • Structure of the extracellular surface of the gap junction by atomic force microscopy
    • Hoh, J. H., Sosinsky, G. E., Revel, J.-P., and Hansma, P. K. (1993). Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys. J. 65, 149-163.
    • (1993) Biophys. J. , vol.65 , pp. 149-163
    • Hoh, J.H.1    Sosinsky, G.E.2    Revel, J.-P.3    Hansma, P.K.4
  • 58
    • 0027138210 scopus 로고
    • Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution
    • Karrasch, S., Dolder, M., Hoh, J., Schaben, F., Ramsden, J., and Engel, A. (1993). Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution. Biophys. J. 65, 2437-2446.
    • (1993) Biophys. J. , vol.65 , pp. 2437-2446
    • Karrasch, S.1    Dolder, M.2    Hoh, J.3    Schaben, F.4    Ramsden, J.5    Engel, A.6
  • 59
    • 0028087275 scopus 로고
    • Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment
    • Karrasch, S., Hegerl, R., Hoh, J., Baumeister, W., and Engel, A. (1994). Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc. Natl. Acad. Sci. U.S.A. 91, 836-838.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 836-838
    • Karrasch, S.1    Hegerl, R.2    Hoh, J.3    Baumeister, W.4    Engel, A.5
  • 61
    • 0027026810 scopus 로고
    • Bacteriorhodopsin reconstituted from two individual helices and the complementary five-helix fragment is photoactive
    • Kataoka, M., Kahn, T. W., Tsujiuchi, Y., Engelman, D. M., and Tokunaga, F. (1992). Bacteriorhodopsin reconstituted from two individual helices and the complementary five-helix fragment is photoactive. Photochem. Photobiol. 56, 895-901.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 895-901
    • Kataoka, M.1    Kahn, T.W.2    Tsujiuchi, Y.3    Engelman, D.M.4    Tokunaga, F.5
  • 63
    • 0020336098 scopus 로고
    • The wrapping phenomenon in airdried and negatively stained preparations
    • Kellenberger, E., Häner, M., and Wurtz, M. (1982). The wrapping phenomenon in airdried and negatively stained preparations. Ultramicroscopy 9, 139-150.
    • (1982) Ultramicroscopy , vol.9 , pp. 139-150
    • Kellenberger, E.1    Häner, M.2    Wurtz, M.3
  • 64
    • 0032034801 scopus 로고    scopus 로고
    • Mechanisms of solute transport through outer membrane porins: Burning down the house
    • Klebba, P. E., and Newton, S. M. (1998). Mechanisms of solute transport through outer membrane porins: burning down the house. Curr. Opin. Microbiol. 1, 238-47.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 238-247
    • Klebba, P.E.1    Newton, S.M.2
  • 65
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch, M. H. J., Dencher, N. A., Oesterhelt, D., Plöhn, H.-J., Rapp, G., and Büldt, G. (1991). Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10, 521-526.
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.H.J.1    Dencher, N.A.2    Oesterhelt, D.3    Plöhn, H.-J.4    Rapp, G.5    Büldt, G.6
  • 66
    • 0023659265 scopus 로고
    • Voltage gating in porin channels
    • Lakey, J. H. (1987). Voltage gating in porin channels. FEBS Lett. 211, 1-4.
    • (1987) FEBS Lett. , vol.211 , pp. 1-4
    • Lakey, J.H.1
  • 67
    • 0029897494 scopus 로고    scopus 로고
    • Porins of Escherichia coli: Uniderectional gating by pressure
    • Le Dain, A.C., Häse, C. C., Tommassen, J., and Martinac, B. (1996). Porins of Escherichia coli: Uniderectional gating by pressure. EMBO J. 15, 3524-3528.
    • (1996) EMBO J. , vol.15 , pp. 3524-3528
    • Le Dain, A.C.1    Häse, C.C.2    Tommassen, J.3    Martinac, B.4
  • 68
    • 0028007197 scopus 로고
    • Direct measurements of the forces between complementary strands of DNA
    • Lee, G. U., Chrisey, L. A., and Colton, R. J. (1994). Direct measurements of the forces between complementary strands of DNA. Science 266, 771-773.
    • (1994) Science , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 69
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee, G. U., Kidwell, D. A., and Colton, R. J. (1994). Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir 10, 354-357.
    • (1994) Langmuir , vol.10 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 70
    • 0021338738 scopus 로고
    • Regeneration of native bacteriorhodopsin structure from fragments
    • Liao, M.-J., Huang, K.-S., and Khorana, H. G. (1984). Regeneration of native bacteriorhodopsin structure from fragments. J. Biol. Chem. 259, 4200-4204.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4200-4204
    • Liao, M.-J.1    Huang, K.-S.2    Khorana, H.G.3
  • 72
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution
    • Luecke, H., Richter, H.-T., and Lanyi, J. K. (1998). Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution. Science 280, 1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 73
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution
    • Luecke, H., Schobert, B., Richter, H.-T., Certailler, J.-P., and Lanyi, J. K. (1999a). Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution. Science 286, 255-260.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Certailler, J.-P.4    Lanyi, J.K.5
  • 75
    • 0031017249 scopus 로고    scopus 로고
    • Direct visualization of supercoiled DNA in situ with atomic force microscopy
    • Lyubchenko, Y. L., and Shlyakhtenko, L. S. (1997). Direct visualization of supercoiled DNA in situ with atomic force microscopy. Proc. Natl. Acad. Sci. U.S.A. 94, 496-501.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 496-501
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2
  • 76
    • 0033105888 scopus 로고    scopus 로고
    • Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy
    • Malghani, M. S., Fang, Y., Cheley, S., Bayley, H., and Yang, J. (1999). Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy. Microsc. Res. Tech. 44, 353-6.
    • (1999) Microsc. Res. Tech. , vol.44 , pp. 353-356
    • Malghani, M.S.1    Fang, Y.2    Cheley, S.3    Bayley, H.4    Yang, J.5
  • 77
    • 0032542229 scopus 로고    scopus 로고
    • Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring
    • Marszalek, P. E., Oberhauser, A. F., Pang, Y. P., and Fernandez, J. M. (1998). Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring. Nature 396, 661-664.
    • (1998) Nature , vol.396 , pp. 661-664
    • Marszalek, P.E.1    Oberhauser, A.F.2    Pang, Y.P.3    Fernandez, J.M.4
  • 78
    • 0028500930 scopus 로고
    • Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopy
    • Martin, J., Goldie, K. N., Engel, A., and Hartl, F. U. (1994). Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopy. Biol. Chem Hoppe-Seyler 375, 635-639.
    • (1994) Biol. Chem Hoppe-Seyler , vol.375 , pp. 635-639
    • Martin, J.1    Goldie, K.N.2    Engel, A.3    Hartl, F.U.4
  • 80
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 a resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka, K., Hirai, T., Murata, K., Miyazawa, A., Kidera, A., Kimura, Y., and Fujiyoshi, Y. (1999). The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol. 286, 861-882.
    • (1999) J. Mol. Biol. , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 81
    • 0141595787 scopus 로고    scopus 로고
    • Tapping mode atomic force microscopy produces faithful high-resolution images of protein surfaces
    • Möller, C., Allen, M., Elings, V., Engel, A., and Müller, D. J. (1999). Tapping mode atomic force microscopy produces faithful high-resolution images of protein surfaces. Biophys. J. 77, 1050-1058.
    • (1999) Biophys. J. , vol.77 , pp. 1050-1058
    • Möller, C.1    Allen, M.2    Elings, V.3    Engel, A.4    Müller, D.J.5
  • 82
    • 0034714159 scopus 로고    scopus 로고
    • Reversible loss of crystallinity on photobleaching purple membrane in presence of hydroxylamine
    • Möller, C., Büldt, G., Dencher, N., Engel, A., and Müller, D. J. (2000). Reversible loss of crystallinity on photobleaching purple membrane in presence of hydroxylamine. J. Mol. Biol. 301, 869-879.
    • (2000) J. Mol. Biol. , vol.301 , pp. 869-879
    • Möller, C.1    Büldt, G.2    Dencher, N.3    Engel, A.4    Müller, D.J.5
  • 83
    • 0030029859 scopus 로고    scopus 로고
    • High resolution surface structure of E. coli GroES oligomer by atomic force microscopy
    • Mou, J., Czajkowsky, D. M., Sheng, S., Ho, R., and Shao, Z. (1996). High resolution surface structure of E. coli GroES oligomer by atomic force microscopy. FEBS Lett. 381, 61-164.
    • (1996) FEBS Lett. , vol.381 , pp. 61-164
    • Mou, J.1    Czajkowsky, D.M.2    Sheng, S.3    Ho, R.4    Shao, Z.5
  • 84
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids
    • Mou, J. X., Yang, J., and Shao, Z. F. (1995). Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J. Mol. Biol. 248, 507-512.
    • (1995) J. Mol. Biol. , vol.248 , pp. 507-512
    • Mou, J.X.1    Yang, J.2    Shao, Z.F.3
  • 85
    • 0028766095 scopus 로고
    • Adhesive forces between ligand and receptor measured by AFM
    • Moy, V. T., Florin, E.-L., and Gaub, H. E. (1994). Adhesive forces between ligand and receptor measured by AFM. Colloids Surf. A93, 343-348.
    • (1994) Colloids Surf. , vol.A93 , pp. 343-348
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 86
    • 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. (1997). Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119, 172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 87
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy
    • Müller, D. J., Baumeister, W., and Engel, A. (1996). Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy. J. Bacterial. 178, 3025-3030.
    • (1996) J. Bacterial. , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 88
    • 0033539578 scopus 로고    scopus 로고
    • Controlled unzipping of a bacterial surface layer with atomic force microscopy
    • Müller, D. J., Baumeister, W., and Engel, A. (1999). Controlled unzipping of a bacterial surface layer with atomic force microscopy. Proc. Natl. Acad. Sci. U.S.A. 96, 13,170-13,174.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 89
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Müller, D. J., Büldt, G., and Engel, A. (1995). Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249, 239-243.
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 90
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Müller, D. J., and Engel, A. (1997). The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73, 1633-1644.
    • (1997) Biophys. J. , vol.73 , pp. 1633-1644
    • Müller, D.J.1    Engel, A.2
  • 91
    • 0037666544 scopus 로고    scopus 로고
    • H and voltage induced structural changes of porin OmpF explain channel closure
    • Müller, D. J., and Engel, A. (1999). pH and voltage induced structural changes of porin OmpF explain channel closure. J. Mol. Biol 285, 1347-1351.
    • (1999) J. Mol. Biol , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 92
    • 0000117845 scopus 로고    scopus 로고
    • The bacteriophage φ29 head-tail connector imaged at high resolution with atomic force microscopy in buffer solution
    • Müller, D. J., Engel, A., Carrascosa, J., and Veléz, M. (1997). The bacteriophage φ29 head-tail connector imaged at high resolution with atomic force microscopy in buffer solution. EMBO J. 16, 101-107.
    • (1997) EMBO J. , vol.16 , pp. 101-107
    • Müller, D.J.1    Engel, A.2    Carrascosa, J.3    Veléz, M.4
  • 93
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the AFM
    • Müller, D. J., Fotiadis, D., and Engel, A. (1998). Mapping flexible protein domains at subnanometer resolution with the AFM. FEBS Lett. 430, 105-111.
    • (1998) FEBS Lett. , vol.430 , pp. 105-111
    • Müller, D.J.1    Fotiadis, D.2    Engel, A.3
  • 94
    • 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. (1999). Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys. J. 76, 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
  • 96
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • Müller, D. J., Sass, H.-J., Müller, S., Büldt, G., and Engel, A. (1999). Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol. Biol. 285, 1903-1909.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1903-1909
    • Müller, D.J.1    Sass, H.-J.2    Müller, S.3    Büldt, G.4    Engel, A.5
  • 97
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at subnanometer resolution by atomic force microscopy
    • Müller, D. J., Schabert, F. A., Büldt, G., and Engel, A. (1995). Imaging purple membranes in aqueous solutions at subnanometer resolution by atomic force microscopy. Biophys. J. 68, 1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Müller, D.J.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 99
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes of native membrane proteins monitored at subnanometer resolution with the atomic force microscope
    • Müller, D. J., Schoenenberger, C.-A., Schabert, F., and Engel, A. (1997). Structural changes of native membrane proteins monitored at subnanometer resolution with the atomic force microscope. J. Struct. Biol. 119, 149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.J.1    Schoenenberger, C.-A.2    Schabert, F.3    Engel, A.4
  • 101
    • 0026458015 scopus 로고
    • Transport proteins in bacteria: Common themes in their design
    • Nikaido, H., and Saier, M. H. (1992). Transport proteins in bacteria: Common themes in their design. Science 258, 936-942.
    • (1992) Science , vol.258 , pp. 936-942
    • Nikaido, H.1    Saier, M.H.2
  • 102
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985). Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49, 1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 104
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., Marszalek, P. E., Erickson, H. P., and Fernandez, J. M. (1998). The molecular elasticity of the extracellular matrix protein tenascin. Nature 393, 181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 105
    • 0016259151 scopus 로고
    • Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: Demonstration of an apo-membrane
    • Oesterhelt, D., Schuhmann, L., and Gruber, H. (1974). Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: Demonstration of an apo-membrane. FEBS Lett. 44, 257-261.
    • (1974) FEBS Lett. , vol.44 , pp. 257-261
    • Oesterhelt, D.1    Schuhmann, L.2    Gruber, H.3
  • 107
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., and Landau, E. M. (1997). X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 108
    • 0023448994 scopus 로고
    • Nucleotide sequence of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies
    • Peters, J., Peters, M., Lottspeich, F., Schäfer, W., and Baumeister, W. (1987). Nucleotide sequence of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies. J. Bacteriol. 169, 5216-5223.
    • (1987) J. Bacteriol. , vol.169 , pp. 5216-5223
    • Peters, J.1    Peters, M.2    Lottspeich, F.3    Schäfer, W.4    Baumeister, W.5
  • 109
    • 0033582948 scopus 로고    scopus 로고
    • Site-directed spin-labelling reveals the orientation of the amino acid side-chains in the E-F loop of bacteriorhodopsin
    • Pfeiffer, M., Rink, T., Gerwert, K., Oesterhelt, D., and Steinhoff, H.-J. (1999). Site-directed spin-labelling reveals the orientation of the amino acid side-chains in the E-F loop of bacteriorhodopsin. J. Mol. Biol. 287, 163-171.
    • (1999) J. Mol. Biol. , vol.287 , pp. 163-171
    • Pfeiffer, M.1    Rink, T.2    Gerwert, K.3    Oesterhelt, D.4    Steinhoff, H.-J.5
  • 111
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle, A., Keller, P., Florin, E. L., Simons, K., and Horber, J. K. (2000). Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell. Biol. 148, 997-1008.
    • (2000) J. Cell. Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 113
    • 0022861964 scopus 로고
    • Projected structure of the surface protein of Deinococcus radiodurans determined to 8 Å resolution by cryomicroscopy
    • Rachel, R., Jakubowski, U., Tietz, H., Hegerl, R., and Baumeister, W. (1986). Projected structure of the surface protein of Deinococcus radiodurans determined to 8 Å resolution by cryomicroscopy. Ultramicroscopy 20, 305-316.
    • (1986) Ultramicroscopy , vol.20 , pp. 305-316
    • Rachel, R.1    Jakubowski, U.2    Tietz, H.3    Hegerl, R.4    Baumeister, W.5
  • 114
    • 0028997572 scopus 로고
    • Imaging soft samples with the atomic force microscope: Gelatin in water and propanol
    • Radmacher, M., Fritz, M., and Hansma, P. K. (1995). Imaging soft samples with the atomic force microscope: Gelatin in water and propanol. Biophys. J. 69, 264-270.
    • (1995) Biophys. J. , vol.69 , pp. 264-270
    • Radmacher, M.1    Fritz, M.2    Hansma, P.K.3
  • 115
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi, V. K., and Girvin, M. E. (1999). Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402, 263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 116
    • 0032919143 scopus 로고    scopus 로고
    • Sequence-dependent mechanics of single DNA molecules
    • Rief, M., Clausen-Schaumann, H., and Gaub, H. (1999). Sequence-dependent mechanics of single DNA molecules. Nat. Struct. Biol. 6, 346-349.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 346-349
    • Rief, M.1    Clausen-Schaumann, H.2    Gaub, H.3
  • 117
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by ARM
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M., and Gaub, H. E. (1997). Reversible unfolding of individual titin immunoglobulin domains by ARM. Science 276, 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
  • 118
    • 0031042739 scopus 로고    scopus 로고
    • Single molecule force spectroscopy on polysaccharides by ARM
    • Rief, M., Oesterhelt, F., Heymann, B., and Gaub, H. E. (1997). Single molecule force spectroscopy on polysaccharides by ARM. Science 275, 1295-1298.
    • (1997) Science , vol.275 , pp. 1295-1298
    • Rief, M.1    Oesterhelt, F.2    Heymann, B.3    Gaub, H.E.4
  • 119
    • 4243277794 scopus 로고    scopus 로고
    • Mapping local electrostatic forces with the atomic force microscope
    • Rotsch, C., and Radmacher, M. (1997). Mapping local electrostatic forces with the atomic force microscope. Langmuir 13, 2825-2832.
    • (1997) Langmuir , vol.13 , pp. 2825-2832
    • Rotsch, C.1    Radmacher, M.2
  • 120
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert, D., Engelbrecht, S., and Junge, W. (1996). Intersubunit rotation in active F-ATPase. Nature 381, 623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 122
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert, F. A., Henn, C., and Engel, A. (1995). Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science 268, 92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 124
    • 0032923225 scopus 로고    scopus 로고
    • Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscopy
    • Scheuring, S., Müller, D. J., Ringler, P., Heymann, J. B., and Engel, A. (1999). Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscopy. J. Microsc. 193, 28-35.
    • (1999) J. Microsc. , vol.193 , pp. 28-35
    • Scheuring, S.1    Müller, D.J.2    Ringler, P.3    Heymann, J.B.4    Engel, A.5
  • 126
    • 0010457541 scopus 로고
    • Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers
    • Schindler, H., and Rosenbusch, J. P. (1978). Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc. Natl. Acad. Sci. U.S.A. 75, 3751-3755.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3751-3755
    • Schindler, H.1    Rosenbusch, J.P.2
  • 127
    • 0019555702 scopus 로고
    • Matrix protein in planar membranes: Clusters of channels in a native environment and their functional assembly
    • Schindler, H., and Rosenbusch, J. P. (1981). Matrix protein in planar membranes: Clusters of channels in a native environment and their functional assembly. Proc. Natl. Acad. Sci. U.S.A. 78, 2302-2306.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2302-2306
    • Schindler, H.1    Rosenbusch, J.P.2
  • 128
    • 0031857538 scopus 로고    scopus 로고
    • General and specific porins from bacterial outer membranes
    • Schirmer, T. (1998). General and specific porins from bacterial outer membranes. J. Stuct. Biol. 121, 101-109.
    • (1998) J. Stuct. Biol. , vol.121 , pp. 101-109
    • Schirmer, T.1
  • 129
    • 0033579482 scopus 로고    scopus 로고
    • Brownian dynamics simulation of ion flow through porin channels
    • Schirmer, T., and Phale, P. S. (1999). Brownian dynamics simulation of ion flow through porin channels. J. Mol. Biol. 294, 1159-1167.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1159-1167
    • Schirmer, T.1    Phale, P.S.2
  • 130
    • 0027640084 scopus 로고
    • Bacterial porins: Structure and function
    • Schulz, G. (1993). Bacterial porins: structure and function. Curr. Opin. Cell Biol. 5, 701-707.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 701-707
    • Schulz, G.1
  • 133
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Shao, Z., Mou, J., Czajkowsky, D. M., Yang, J., and Yuan, J.-Y. (1996). Biological atomic force microscopy: what is achieved and what is needed. Adv. Phys. 45, 1-86.
    • (1996) Adv. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.-Y.5
  • 136
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 137
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: An overview
    • Sleytr, U. B. (1997). Basic and applied S-layer research: an overview. FEMS Microbiol. Rev. 20, 5-12.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 138
    • 0027318079 scopus 로고
    • Crystalline bacterial cell surface layers: General principles and application potential
    • Sleytr, U. B., Messner, P., Pum, D., and Sára, M. (1993). Crystalline bacterial cell surface layers: general principles and application potential. J. Appl. Bacteriol. Symp. Suppl. 74, 21S-32S.
    • (1993) J. Appl. Bacteriol. Symp. Suppl. , vol.74
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sára, M.4
  • 139
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith, S. B., Cui, Y., and Bustamante, C. (1996). Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules. Science 271, 795-798.
    • (1996) Science , vol.271 , pp. 795-798
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 140
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996). Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 141
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A. G., and Walker, J. E. (1999). Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 143
    • 0020402321 scopus 로고
    • The association of the surface array and the outer membrane of Deinococcus radiodurans
    • Thompson, B. G., Murray, R. G. E., and Boyce, J. F. (1982). The association of the surface array and the outer membrane of Deinococcus radiodurans. Can. J. Microbiol. 28, 1081-1088.
    • (1982) Can. J. Microbiol. , vol.28 , pp. 1081-1088
    • Thompson, B.G.1    Murray, R.G.E.2    Boyce, J.F.3
  • 144
    • 0026474470 scopus 로고
    • Effects of pH on bacterial porin function
    • Todt, J. C., Rocque, W. J., and McGroarty, E. J. (1992). Effects of pH on bacterial porin function. Biochemistry 31, 10,471-10,478.
    • (1992) Biochemistry , vol.31
    • Todt, J.C.1    Rocque, W.J.2    McGroarty, E.J.3
  • 145
    • 0021645447 scopus 로고
    • Multivariate statistical classification of noise images (randomly orientated biological macromolecules)
    • van Heel, M. (1984). Multivariate statistical classification of noise images (randomly orientated biological macromolecules). Ultramicroscopy 13, 165-184.
    • (1984) Ultramicroscopy , vol.13 , pp. 165-184
    • Van Heel, M.1
  • 147
    • 0030596147 scopus 로고    scopus 로고
    • Surface topographies at subnanometer-resolution reveal asymmetry and sidedness of aquaporin-1
    • Walz, T., Tiltmann, P., Fuchs, K. H., Müller, D. J., Smith, B. L., Agre, P., Gross, H., and Engel, A. (1996). Surface topographies at subnanometer-resolution reveal asymmetry and sidedness of aquaporin-1. J. Mol. Biol. 264, 907-918.
    • (1996) J. Mol. Biol. , vol.264 , pp. 907-918
    • Walz, T.1    Tiltmann, P.2    Fuchs, K.H.3    Müller, D.J.4    Smith, B.L.5    Agre, P.6    Gross, H.7    Engel, A.8
  • 148
    • 36448999468 scopus 로고
    • Limits of imaging resolution for atomic force microscopy of molecules
    • Weihs, T. P., Nawaz, Z., Jams, S. P., and Pethica, J. B. (1991). Limits of imaging resolution for atomic force microscopy of molecules. Apl. Phys. Lett. 59, 3536-3538.
    • (1991) Apl. Phys. Lett. , vol.59 , pp. 3536-3538
    • Weihs, T.P.1    Nawaz, Z.2    Jams, S.P.3    Pethica, J.B.4
  • 149
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M. S., Abele, U., Weckesser, J., Welte, W., Schlitz, E., and Schulz, G. E. (1991). Molecular architecture and electrostatic properties of a bacterial porin. Science 254, 1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schlitz, E.5    Schulz, G.E.6
  • 150
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H., and Wimley, W. C. (1999). Membrane protein folding and stability: Physical principles. Annu. Rev. Biophys. Biomol. Struct. 28, 319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 151
    • 0028970620 scopus 로고
    • Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. A. (1995). Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2, 961-967.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 961-967
    • Wilkens, S.1    Dahlquist, F.W.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 152
    • 0031055743 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase
    • Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W., and Capaldi, R. A. (1997). Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase. Nat. Struct. Biol. 4, 198-201.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 198-201
    • Wilkens, S.1    Dunn, S.D.2    Chandler, J.3    Dahlquist, F.W.4    Capaldi, R.A.5
  • 153
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins
    • Yang, J., Tamm, L. K., Tillack, T. W., and Shao, Z. (1993). New approach for atomic force microscopy of membrane proteins. J. Mol. Biol. 229, 286-290.
    • (1993) J. Mol. Biol. , vol.229 , pp. 286-290
    • Yang, J.1    Tamm, L.K.2    Tillack, T.W.3    Shao, Z.4
  • 154
    • 0027610690 scopus 로고
    • Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy
    • Zhong, Q., Inniss, D., Kjoller, K., and Elings, V. B. (1993). Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy. Surf. Sci. Lett. 290, L688-692.
    • (1993) Surf. Sci. Lett. , vol.290
    • Zhong, Q.1    Inniss, D.2    Kjoller, K.3    Elings, V.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.