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Volumn 88, Issue 2, 2005, Pages 1423-1431

Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; GLOBULAR PROTEIN; MEMBRANE PROTEIN;

EID: 21244500106     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.052746     Document Type: Article
Times cited : (66)

References (47)
  • 1
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 2
    • 0034804341 scopus 로고    scopus 로고
    • Can nonmechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R. B., B. Li, A. Steward, V. Daggett, and J. Clarke. 2001. Can nonmechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2344-2356.
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 4
    • 0031302710 scopus 로고    scopus 로고
    • Folding alpha-helical membrane proteins: Kinetic studies on bacteriorhodopsin
    • Booth, P. J. 1997. Folding alpha-helical membrane proteins: kinetic studies on bacteriorhodopsin. Fold. Des. 2:R85-R92.
    • (1997) Fold. Des. , vol.2
    • Booth, P.J.1
  • 5
    • 0034872196 scopus 로고    scopus 로고
    • Can we identify the forces that drive the folding of integral membrane proteins?
    • Booth, P. J., R. H. Templer, A. R. Curran, and S. J. Allen. 2001. Can we identify the forces that drive the folding of integral membrane proteins? Biochem. Soc. T. 29:408-413.
    • (2001) Biochem. Soc. T. , vol.29 , pp. 408-413
    • Booth, P.J.1    Templer, R.H.2    Curran, A.R.3    Allen, S.J.4
  • 6
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt, H. J., and M. Jaschke. 1995. Calculation of thermal noise in atomic force microscopy. Nanotechnology. 6:1-7.
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2
  • 7
    • 1142310673 scopus 로고    scopus 로고
    • Force spectroscopy with a small dithering of AFM tip: A method of direct and continuous measurement of the spring constant of single molecules and molecular complexes
    • Chtcheglova, L. A., G. T. Shubeita, S. K. Sekatskii, and G. Dietler. 2004. Force spectroscopy with a small dithering of AFM tip: a method of direct and continuous measurement of the spring constant of single molecules and molecular complexes. Biophys. J. 86:1177-1184.
    • (2004) Biophys. J. , vol.86 , pp. 1177-1184
    • Chtcheglova, L.A.1    Shubeita, G.T.2    Sekatskii, S.K.3    Dietler, G.4
  • 8
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of nolecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • In press
    • Cisneros, D., D. Oesterhelt, and D. J. Müller. 2005. Probing origins of nolecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure. In press.
    • (2005) Structure
    • Cisneros, D.1    Oesterhelt, D.2    Müller, D.J.3
  • 9
    • 1642385943 scopus 로고    scopus 로고
    • Lorentz-force-induced excitation of cantilevers for oscillation-mode scanning probe microscopy
    • Enders, O., F. Korte, and H. A. Kolb. 2004. Lorentz-force-induced excitation of cantilevers for oscillation-mode scanning probe microscopy. Surf. Int. Anal. 36:119-123.
    • (2004) Surf. Int. Anal. , vol.36 , pp. 119-123
    • Enders, O.1    Korte, F.2    Kolb, H.A.3
  • 10
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L., R. Siegert, W. D. Lehmann, and D. Oesterhelt. 1998. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. USA. 95:11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 13
    • 0001116334 scopus 로고    scopus 로고
    • A magnetically driven oscillating probe microscope for operation in liquids
    • Han, W. H., S. M. Lindsay, and T. W. Jing. 1996. A magnetically driven oscillating probe microscope for operation in liquids. Appl. Phys. Lett. 69:4111-4113.
    • (1996) Appl. Phys. Lett. , vol.69 , pp. 4111-4113
    • Han, W.H.1    Lindsay, S.M.2    Jing, T.W.3
  • 14
    • 0035945151 scopus 로고    scopus 로고
    • Energy dissipation in atomic force microscopy and atomic loss processes
    • Hoffmann, P. M., S. Jeffery, J. B. Pethica, H. O. Ozer, and A. Oral. 2001. Energy dissipation in atomic force microscopy and atomic loss processes. Phys. Rev. Lett. 87:265502-265504.
    • (2001) Phys. Rev. Lett. , vol.87 , pp. 265502-265504
    • Hoffmann, P.M.1    Jeffery, S.2    Pethica, J.B.3    Ozer, H.O.4    Oral, A.5
  • 15
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang, K. S., H. Bayley, M. J. Liao, E. London, and H. G. Khorana. 1981. Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem. 256:3802-3809.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 16
    • 0034300937 scopus 로고    scopus 로고
    • Active quality factor control in liquids for force spectroscopy
    • Humphris, A. D. L., J. Tamayo, and M. J. Miles. 2000. Active quality factor control in liquids for force spectroscopy. Langmuir. 16:7891-7894.
    • (2000) Langmuir , vol.16 , pp. 7891-7894
    • Humphris, A.D.L.1    Tamayo, J.2    Miles, M.J.3
  • 17
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • Janovjak, H., M. Kessler, D. Oesterhelt, H. E. Gaub, and D. J. Müller. 2003. Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J. 22:5220-5229.
    • (2003) EMBO J. , vol.22 , pp. 5220-5229
    • Janovjak, H.1    Kessler, M.2    Oesterhelt, D.3    Gaub, H.E.4    Müller, D.J.5
  • 19
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov, A., C. Ziegler, H. Janovjak, W. Kühlbrandt, and D. J. Müller. 2004. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 340:1143-1152.
    • (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
  • 21
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution
    • Kolbe, M., H. Besir, L. O. Essen, and D. Oesterhelt. 2000. Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science. 288:1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 22
    • 30244570624 scopus 로고
    • Scanning tunneling microscopy and atomic force microscopy studies of biomaterials at a liquid-solid interface
    • Lindsay, S. M., Y. L. Lyubchenko, N. J. Tao, Y. Q. Li, P. I. Oden, J. A. DeRose, and J. Pan. 1993. Scanning tunneling microscopy and atomic force microscopy studies of biomaterials at a liquid-solid interface. J. Vac. Sci. Technol A. 11:808-815.
    • (1993) J. Vac. Sci. Technol. A , vol.11 , pp. 808-815
    • Lindsay, S.M.1    Lyubchenko, Y.L.2    Tao, N.J.3    Li, Y.Q.4    Oden, P.I.5    Derose, J.A.6    Pan, J.7
  • 23
    • 0033308937 scopus 로고    scopus 로고
    • Relationship between stiffness and force in single molecule pulling experiments
    • Liu, Y. Z., S. H. Leuba, and S. M. Lindsay. 1999. Relationship between stiffness and force in single molecule pulling experiments. Langmuir. 14:8547-8548.
    • (1999) Langmuir , vol.14 , pp. 8547-8548
    • Liu, Y.Z.1    Leuba, S.H.2    Lindsay, S.M.3
  • 26
    • 0029665047 scopus 로고    scopus 로고
    • Mechanical unfolding of alpha(2)-macroglobulin molecules with atomic force microscope
    • Mitsui, K., M. Hara, and A. Ikai. 1996. Mechanical unfolding of alpha(2)-macroglobulin molecules with atomic force microscope. FEBS Lett. 385:29-33.
    • (1996) FEBS Lett. , vol.385 , pp. 29-33
    • Mitsui, K.1    Hara, M.2    Ikai, A.3
  • 28
    • 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., T. Hirai, K. Murata, A. Miyazawa, A. Kidera, Y. Kimura, and Y. Fujiyoshi. 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
  • 30
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller, D. J., M. Amrein, and A. Engel. 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
  • 31
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
    • Müller, D. J., M. Kessler, F. Oesterhelt, C. Möller, D. Oesterhelt, and H. Gaub. 2002. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83:3578-3588.
    • (2002) Biophys. J. , vol.83 , pp. 3578-3588
    • Müller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Möller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 32
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy
    • Müller, D. J., F. A. Schaben, G. Büldt, and A. Engel. 1995. Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys. J. 68:1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Müller, D.J.1    Schaben, F.A.2    Büldt, G.3    Engel, A.4
  • 33
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 35
    • 1042267431 scopus 로고    scopus 로고
    • Dynamics of a partially stretched protein molecule studied using an atomic force microscope
    • Okajima, T., H. Arakawa, M. T. Alam, H. Sekiguchi, and A. Ikai. 2004. Dynamics of a partially stretched protein molecule studied using an atomic force microscope. Biophys. Chem. 107:51-61.
    • (2004) Biophys. Chem. , vol.107 , pp. 51-61
    • Okajima, T.1    Arakawa, H.2    Alam, M.T.3    Sekiguchi, H.4    Ikai, A.5
  • 36
    • 79960670145 scopus 로고
    • Tip surface interactions in STM and AFM
    • Pethica, J. B., and W. C. Oliver. 1987. Tip surface interactions in STM and AFM. Phys. Scripta. T19 A:61-66.
    • (1987) Phys. Scripta , vol.T19A , pp. 61-66
    • Pethica, J.B.1    Oliver, W.C.2
  • 37
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
    • Popot, J. L., S. E. Gerchman, and D. M. Engelman. 1987. Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J. Mol. Biol 198:655-676.
    • (1987) J. Mol. Biol , vol.198 , pp. 655-676
    • Popot, J.L.1    Gerchman, S.E.2    Engelman, D.M.3
  • 39
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: Progress made and promises ahead
    • Radford, S. E. 2000. Protein folding: progress made and promises ahead. Trends Biochem. Sci. 25:611-618.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.E.1
  • 40
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., C. M. Dobson, and P. A. Evans. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 41
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. 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
  • 44
    • 85030794491 scopus 로고
    • Sinusoidal loading and the mechanical loss measurement, in
    • N. R. Amundson, editor. Prentice Hall, Englewood Cliffs, NJ
    • Schultz, J. M. 1974. Sinusoidal loading and the mechanical loss measurement, in Polymer Materials Science. N. R. Amundson, editor. Prentice Hall, Englewood Cliffs, NJ. 371-379.
    • (1974) Polymer Materials Science , pp. 371-379
    • Schultz, J.M.1
  • 45
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J. S., and P. S. Kim. 1991. Reexamination of the folding of BPTI: predominance of native intermediates. Science. 253:1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 47
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • Yohannan, S., S. Faham, D. Yang, J. P. Whitelegge, and J. U. Bowie. 2003. The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors. Proc. Natl. Acad. Sci. USA. 101:959-963.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5


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