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Volumn 93, Issue 6, 2007, Pages 2024-2037

Electrostatic and steric interactions determine bacteriorhodopsin single-molecule biomechanics

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; HALORHODOPSIN; PROTON PUMP; TRYPTOPHAN;

EID: 34548767173     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.101469     Document Type: Article
Times cited : (9)

References (84)
  • 1
    • 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
  • 2
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 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
  • 4
    • 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. Kuhlbrandt, 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    Kuhlbrandt, W.4    Müller, D.J.5
  • 5
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • Janovjak, H., M. Kessler, D. Oesterhelt, H. 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.4    Müller, D.J.5
  • 8
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros, D. A., D. Oesterhelt, and D. J. Müller. 2005. Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure. 13:235-242.
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Müller, D.J.3
  • 9
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin a-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 a-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
  • 10
    • 33644844356 scopus 로고    scopus 로고
    • Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM
    • Kessler, M., and H. E. Gaub. 2006. Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM. Structure. 14:521-527.
    • (2006) Structure , vol.14 , pp. 521-527
    • Kessler, M.1    Gaub, H.E.2
  • 11
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat. New Biol. 233:149-152.
    • (1971) Nat. New Biol , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 12
    • 21244499919 scopus 로고
    • Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
    • Kates, M., S. C. Kushwaha, and G. D. Sprott. 1982. Lipids of purple membrane from extreme halophiles and of methanogenic bacteria. Meth. Enzymol. 88:98-111.
    • (1982) Meth. Enzymol , vol.88 , pp. 98-111
    • Kates, M.1    Kushwaha, S.C.2    Sprott, G.D.3
  • 13
    • 0036164090 scopus 로고    scopus 로고
    • Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane
    • Corcelli, A., V. M. T. Lattanzio, G. Mascolo, P. Papadia, and F. Fanizzi. 2002. Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane. J. Lipid Res. 43:132-140.
    • (2002) J. Lipid Res , vol.43 , pp. 132-140
    • Corcelli, A.1    Lattanzio, V.M.T.2    Mascolo, G.3    Papadia, P.4    Fanizzi, F.5
  • 16
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å 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 Å 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
  • 17
    • 0037285261 scopus 로고    scopus 로고
    • Structural clues to the mechanism of ion pumping in bacteriorhodopsin
    • Luecke, H., and J. K. Lanyi. 2003. Structural clues to the mechanism of ion pumping in bacteriorhodopsin. Adv. Protein Chem.63:111-130.
    • (2003) Adv. Protein Chem , vol.63 , pp. 111-130
    • Luecke, H.1    Lanyi, J.K.2
  • 18
    • 0041352147 scopus 로고    scopus 로고
    • X-ray and crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane
    • Cartailler, J. P., and H. Luecke. 2003. X-ray and crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane. Annu. Rev. Biophys. Biomol. Struct. 32:285-310.
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 285-310
    • Cartailler, J.P.1    Luecke, H.2
  • 19
    • 0029057198 scopus 로고
    • Bacteriorhodopsin as a model for proton pumps
    • Lanyi, J. K. 1995. Bacteriorhodopsin as a model for proton pumps. Nature. 375:461-463.
    • (1995) Nature , vol.375 , pp. 461-463
    • Lanyi, J.K.1
  • 20
    • 25144504440 scopus 로고    scopus 로고
    • A microprobe analysis of inorganic elements in Halobacterium salinarum
    • Engel, M. B., and H. R. Catchpole. 2005. A microprobe analysis of inorganic elements in Halobacterium salinarum. Cell Biol. Intl. 29:616-622.
    • (2005) Cell Biol. Intl , vol.29 , pp. 616-622
    • Engel, M.B.1    Catchpole, H.R.2
  • 21
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • Madern, D., C. Ebel, and G. Zaccai. 2000. Halophilic adaptation of enzymes. Extremophiles. 4:91-98.
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 22
    • 0036596632 scopus 로고    scopus 로고
    • Amino acid composition of bulk protein and salt relationships of selected enzymes of Salinibacter ruber, an extremely halophilic bacterium
    • Oren, A., and L. Mana. 2004. Amino acid composition of bulk protein and salt relationships of selected enzymes of Salinibacter ruber, an extremely halophilic bacterium. Extremophiles. 6:217-223.
    • (2004) Extremophiles , vol.6 , pp. 217-223
    • Oren, A.1    Mana, L.2
  • 23
    • 33645545806 scopus 로고    scopus 로고
    • Differential stiffness and lipid mobility in the leaflets of purple membranes
    • Voïtchovsky, K., S. Antoranz Contera, M. Kamihira, A. Watts, and J. F. Ryan. 2006. Differential stiffness and lipid mobility in the leaflets of purple membranes. Biophys. J. 90:2075-2085.
    • (2006) Biophys. J , vol.90 , pp. 2075-2085
    • Voïtchovsky, K.1    Antoranz Contera, S.2    Kamihira, M.3    Watts, A.4    Ryan, J.F.5
  • 24
    • 0029665047 scopus 로고    scopus 로고
    • 2-macroglobulin molecules with atomic force microscope
    • 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
  • 25
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S. Z., S. B. Smith, H. L. Granzier, and C. Bustamante. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 30
    • 27744539797 scopus 로고    scopus 로고
    • Mechanical unfolding of ubiquitin molecules
    • Cieplak, M., and P. E. Marszalek. 2005. Mechanical unfolding of ubiquitin molecules. J. Chem. Phys. 123:194903.
    • (2005) J. Chem. Phys , vol.123 , pp. 194903
    • Cieplak, M.1    Marszalek, P.E.2
  • 32
    • 0036385794 scopus 로고    scopus 로고
    • The backbone conformational entropy of protein folding: Experimental measures from atomic force microscopy
    • Thompson, J. B., H. G. Hansma, P. K. Hansma, and K. W. Plaxco. 2002. The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy. J. Mol. Biol. 322:645-652.
    • (2002) J. Mol. Biol , vol.322 , pp. 645-652
    • Thompson, J.B.1    Hansma, H.G.2    Hansma, P.K.3    Plaxco, K.W.4
  • 34
    • 27744527489 scopus 로고    scopus 로고
    • Unfolding and extraction of a transmembrane α-helical peptide: Dynamic force spectroscopy and molecular dynamics simulations
    • Antoranz Contera, S., V. Lemaître, M. R. R. de Planque, A. Watts, and J. F. Ryan. 2005. Unfolding and extraction of a transmembrane α-helical peptide: dynamic force spectroscopy and molecular dynamics simulations. Biophys. J. 89:3129-3140.
    • (2005) Biophys. J , vol.89 , pp. 3129-3140
    • Antoranz Contera, S.1    Lemaître, V.2    de Planque, M.R.R.3    Watts, A.4    Ryan, J.F.5
  • 35
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra, K. T., H. Besir, D. Oesterhelt, and D. J. Müller. 2006. Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355:640-650.
    • (2006) J. Mol. Biol , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Müller, D.J.4
  • 37
    • 85030500847 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 38
    • 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
  • 39
    • 36449007507 scopus 로고
    • Parallel beam approximation for V-shaped atomic force microscope cantilevers
    • Sader, J. E. 1995. Parallel beam approximation for V-shaped atomic force microscope cantilevers. Rev. Sci. Instr. 66:4583-4587.
    • (1995) Rev. Sci. Instr , vol.66 , pp. 4583-4587
    • Sader, J.E.1
  • 41
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. 2003. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta. 1612:1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 42
    • 0342980347 scopus 로고    scopus 로고
    • Determination of iso-electric point of silicon nitride by adhesion method
    • Biscan, J., N. Kallay, and T. Smolic. 2000. Determination of iso-electric point of silicon nitride by adhesion method. Colloids Surf. A. 165:115-123.
    • (2000) Colloids Surf. A , vol.165 , pp. 115-123
    • Biscan, J.1    Kallay, N.2    Smolic, T.3
  • 43
    • 0024978461 scopus 로고
    • Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin
    • Mogi, T., T. Marti, and H. G. Khorana. 1989. Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin. J. Biol. Chem. 264:14197-14201.
    • (1989) J. Biol. Chem , vol.264 , pp. 14197-14201
    • Mogi, T.1    Marti, T.2    Khorana, H.G.3
  • 44
    • 0033919167 scopus 로고    scopus 로고
    • Bacteriorhodopsin thermal stability: Influence of bound cations and lipids on the intrinsic protein fluorescence
    • Tuparev, N., A. Dobrikova, S. Taneva, and T. Lazarova. 2000. Bacteriorhodopsin thermal stability: influence of bound cations and lipids on the intrinsic protein fluorescence. Zeitschrift fur Naturforschung. C. 55:355-360.
    • (2000) Zeitschrift fur Naturforschung. C , vol.55 , pp. 355-360
    • Tuparev, N.1    Dobrikova, A.2    Taneva, S.3    Lazarova, T.4
  • 45
    • 0026753574 scopus 로고
    • Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin
    • Wu, S., Y. Chang, M. A. el-Sayed, T. Marti, T. Mogi, and H. G. Khorana. 1992. Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin. Biophys. J. 61:1281-1288.
    • (1992) Biophys. J , vol.61 , pp. 1281-1288
    • Wu, S.1    Chang, Y.2    el-Sayed, M.A.3    Marti, T.4    Mogi, T.5    Khorana, H.G.6
  • 46
    • 23244431748 scopus 로고    scopus 로고
    • Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin
    • Schenkl, S., F. van Mourik, G. van der Zwan, S. Haacke, and M. Chergui. 2005. Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin. Science. 309:917-920.
    • (2005) Science , vol.309 , pp. 917-920
    • Schenkl, S.1    van Mourik, F.2    van der Zwan, G.3    Haacke, S.4    Chergui, M.5
  • 49
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Ångströms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, and E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 Ångströms 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
  • 50
    • 0024976553 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Chromophore isomerization perturbs tryptophan-86
    • Rothschild, K. J., D. Gray, T. Mogi, T. Marti, M. S. Braiman, L. J. Stern, and H. G. Khorana. 1989. Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86. Biochemistry. 28:7052-7059.
    • (1989) Biochemistry , vol.28 , pp. 7052-7059
    • Rothschild, K.J.1    Gray, D.2    Mogi, T.3    Marti, T.4    Braiman, M.S.5    Stern, L.J.6    Khorana, H.G.7
  • 51
    • 0019302483 scopus 로고
    • Light isomerizes the chromophore of bacteriorhodopsin
    • Tsuda, M., M. Glaccum, B. Nelson, and T. G. Ebrey. 1980. Light isomerizes the chromophore of bacteriorhodopsin. Nature. 287:351-353.
    • (1980) Nature , vol.287 , pp. 351-353
    • Tsuda, M.1    Glaccum, M.2    Nelson, B.3    Ebrey, T.G.4
  • 52
    • 22144459357 scopus 로고    scopus 로고
    • Ultrafast excited state dynamics of the protonated Schiff base of all-trans retinal in solvents
    • Zgrablic, G., K. Voïtchovsky, M. Kindermann, S. Haacke, and M. Chergui. 2005. Ultrafast excited state dynamics of the protonated Schiff base of all-trans retinal in solvents. Biophys. J. 88:2779-2788.
    • (2005) Biophys. J , vol.88 , pp. 2779-2788
    • Zgrablic, G.1    Voïtchovsky, K.2    Kindermann, M.3    Haacke, S.4    Chergui, M.5
  • 53
    • 0034315814 scopus 로고    scopus 로고
    • Electrostatic protein-chromophore interactions promote the all-trans → 13-cis isomerization of the protonated retinal Schiff base in bacteriorhodopsin: An ab initio CASSCF/MRCI study
    • Nonella, M. 2000. Electrostatic protein-chromophore interactions promote the all-trans → 13-cis isomerization of the protonated retinal Schiff base in bacteriorhodopsin: an ab initio CASSCF/MRCI study. J. Phys. Chem. B. 104:11379-11388.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11379-11388
    • Nonella, M.1
  • 54
    • 0001092509 scopus 로고
    • A comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal
    • Becker, R. S., and K. Freedman. 1985. A comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal. J. Am. Chem. Soc. 107:1477-1485.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 1477-1485
    • Becker, R.S.1    Freedman, K.2
  • 55
    • 0029738907 scopus 로고    scopus 로고
    • Steric interaction between the 9-methyl group of the retinal and Tryptophan 182 controls 13-cis to all-trans re-isomerization and proton uptake in the bacteriorhodopsin photocycle
    • Weidlich, O., B. Schalt, N. Friedman, M. Sheves, J. K. Lanyi, L. S. Brown, and F. Siebert. 1996. Steric interaction between the 9-methyl group of the retinal and Tryptophan 182 controls 13-cis to all-trans re-isomerization and proton uptake in the bacteriorhodopsin photocycle. Biochemistry. 35:10807-10814.
    • (1996) Biochemistry , vol.35 , pp. 10807-10814
    • Weidlich, O.1    Schalt, B.2    Friedman, N.3    Sheves, M.4    Lanyi, J.K.5    Brown, L.S.6    Siebert, F.7
  • 57
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R. R., and J. A. Killian. 2003. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membr. Biol. 20:271-284.
    • (2003) Mol. Membr. Biol , vol.20 , pp. 271-284
    • de Planque, M.R.R.1    Killian, J.A.2
  • 58
    • 0037008040 scopus 로고    scopus 로고
    • The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane a-helical peptides depend on the nature of interfacially exposed aromatic and charged residues
    • de Planque, M. R. R., J. W. P. Boots, D. T. S. Rijkers, R. M. J. Liskamp, D. V. Greathouse, and J. A. Killian. 2002. The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane a-helical peptides depend on the nature of interfacially exposed aromatic and charged residues. Biochemistry. 41:8396-8404.
    • (2002) Biochemistry , vol.41 , pp. 8396-8404
    • de Planque, M.R.R.1    Boots, J.W.P.2    Rijkers, D.T.S.3    Liskamp, R.M.J.4    Greathouse, D.V.5    Killian, J.A.6
  • 59
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque, M. R. R., B. B. Bonev, J. A. A. Demmers, D. V. Greathouse, R. E. Koeppe, F. Separovic, A. Watts, and J. A. Killian. 2003. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry. 42:5341-5348.
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • de Planque, M.R.R.1    Bonev, B.B.2    Demmers, J.A.A.3    Greathouse, D.V.4    Koeppe, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8
  • 60
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force, lifetime, and chemistry in single molecular bonds
    • Evans, E. 2001. Probing the relation between force, lifetime, and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30:105-128.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 105-128
    • Evans, E.1
  • 61
    • 0141816804 scopus 로고    scopus 로고
    • Beyond the conventional description of dynamic force spectroscopy of adhesion bonds
    • Dudko, O. K., A. E. Filippov, J. Klafter, and M. Urbakh. 2003. Beyond the conventional description of dynamic force spectroscopy of adhesion bonds. Proc. Natl. Acad. Sci. USA. 100:11378-11381.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11378-11381
    • Dudko, O.K.1    Filippov, A.E.2    Klafter, J.3    Urbakh, M.4
  • 62
    • 0037150073 scopus 로고    scopus 로고
    • Changes in hydrogen bonding and environment of tryptophan residues on helix F of bacteriorhodopsin during the photocycle: A time-resolved ultraviolet resonance Raman study
    • Hashimoto, S., M. Sasaki, H. Takeuchi, R. Needleman, and J. K. Lanyi. 2002. Changes in hydrogen bonding and environment of tryptophan residues on helix F of bacteriorhodopsin during the photocycle: a time-resolved ultraviolet resonance Raman study. Biochemistry. 41:6495-6503.
    • (2002) Biochemistry , vol.41 , pp. 6495-6503
    • Hashimoto, S.1    Sasaki, M.2    Takeuchi, H.3    Needleman, R.4    Lanyi, J.K.5
  • 63
    • 0023393593 scopus 로고
    • Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation
    • Mogi, T., L. J. Stern, N. R. Hackett, and H. G. Khorana. 1987. Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation. Proc. Natl. Acad. Sci. USA. 84:5595-5599.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5595-5599
    • Mogi, T.1    Stern, L.J.2    Hackett, N.R.3    Khorana, H.G.4
  • 66
    • 0035798539 scopus 로고    scopus 로고
    • Contribution of extracellular Glu residues to the structure and function of bacteriorhodopsin: Presence of specific cation binding sites
    • Sanz, C., M. Marquez, A. Peralvarez, S. Elouatik, F. Sepulcre, E. Querol, T. Lazarova, and E. Padros. 2001. Contribution of extracellular Glu residues to the structure and function of bacteriorhodopsin: presence of specific cation binding sites. J. Biol. Chem. 276:40788-40794.
    • (2001) J. Biol. Chem , vol.276 , pp. 40788-40794
    • Sanz, C.1    Marquez, M.2    Peralvarez, A.3    Elouatik, S.4    Sepulcre, F.5    Querol, E.6    Lazarova, T.7    Padros, E.8
  • 67
    • 0030808219 scopus 로고    scopus 로고
    • Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    • Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry. 36:8671-8676.
    • (1997) Biochemistry , vol.36 , pp. 8671-8676
    • Balashov, S.P.1    Imasheva, E.S.2    Ebrey, T.G.3    Chen, N.4    Menick, D.R.5    Crouch, R.K.6
  • 68
    • 14844347271 scopus 로고    scopus 로고
    • Proton binding within a membrane protein by a protonated water cluster
    • Garczarek, F., L. S. Brown, J. K. Lanyi, and K. Gerwert. 2005. Proton binding within a membrane protein by a protonated water cluster. Proc. Natl. Acad. Sci. USA. 102:3633-3638.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3633-3638
    • Garczarek, F.1    Brown, L.S.2    Lanyi, J.K.3    Gerwert, K.4
  • 69
    • 0028102402 scopus 로고
    • Proton migration along the membrane surface and retarded surface to bulk transfer
    • Heberle, J., J. Riesle, G. Thiedemann, D. Oesterhelt, and N. A. Dencher. 1994. Proton migration along the membrane surface and retarded surface to bulk transfer. Nature. 370:379-382.
    • (1994) Nature , vol.370 , pp. 379-382
    • Heberle, J.1    Riesle, J.2    Thiedemann, G.3    Oesterhelt, D.4    Dencher, N.A.5
  • 70
    • 33751213903 scopus 로고    scopus 로고
    • Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membrane
    • Seeber, M., F. Fanelli, E. Paci, and A. Caflisch. 2006. Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membrane. Biophys. J. 91:3276-3284.
    • (2006) Biophys. J , vol.91 , pp. 3276-3284
    • Seeber, M.1    Fanelli, F.2    Paci, E.3    Caflisch, A.4
  • 71
    • 0031013660 scopus 로고    scopus 로고
    • Mutation of a surface residue, Lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin. Guanidine hydrochloride restores it
    • Govindjee, R., E. S. Imasheva, S. Misra, S. P. Balashov, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Mutation of a surface residue, Lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin. Guanidine hydrochloride restores it. Biophys. J. 72:886-898.
    • (1997) Biophys. J , vol.72 , pp. 886-898
    • Govindjee, R.1    Imasheva, E.S.2    Misra, S.3    Balashov, S.P.4    Ebrey, T.G.5    Chen, N.6    Menick, D.R.7    Crouch, R.K.8
  • 72
    • 0029744105 scopus 로고    scopus 로고
    • Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane
    • Nachliel, E., M. Gutman, S. Kiryati, and N. A. Dencher. 1996. Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane. Proc. Natl. Acad. Sci. USA. 93:10747-10752.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10747-10752
    • Nachliel, E.1    Gutman, M.2    Kiryati, S.3    Dencher, N.A.4
  • 73
    • 0000830257 scopus 로고
    • The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin
    • Blanck, A., and D. Oesterhelt. 1987. The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J. 6:265-273.
    • (1987) EMBO J , vol.6 , pp. 265-273
    • Blanck, A.1    Oesterhelt, D.2
  • 74
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Váró, G. 2000. Analogies between halorhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta. 1460:220-229.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Váró, G.1
  • 75
    • 0029886089 scopus 로고    scopus 로고
    • A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: Part of the F helix tilts in the M to N transition
    • Vonck, J. 1996. A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition. Biochemistry. 35:5870-5878.
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 76
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand, M., A. J. Dianoux, W. Petry, and G. Zaccai. 1993. Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 77
    • 0031990356 scopus 로고    scopus 로고
    • Localization of glycolipids in membranes by in vivo labeling and neutron diffraction
    • Weik, M., H. Patzelt, G. Zaccai, and D. Oesterhelt. 1998. Localization of glycolipids in membranes by in vivo labeling and neutron diffraction. Mol. Cell. 1:411-419.
    • (1998) Mol. Cell , vol.1 , pp. 411-419
    • Weik, M.1    Patzelt, H.2    Zaccai, G.3    Oesterhelt, D.4
  • 78
    • 0018187260 scopus 로고
    • Specific labeling of the protein and lipid on the extracellular surface of purple membrane
    • Henderson, R., J. S. Jubb, and S. Whytock. 1978. Specific labeling of the protein and lipid on the extracellular surface of purple membrane. J. Mol. Biol. 123:259-274.
    • (1978) J. Mol. Biol , vol.123 , pp. 259-274
    • Henderson, R.1    Jubb, J.S.2    Whytock, S.3
  • 79
    • 0033551432 scopus 로고    scopus 로고
    • Role of helix-helix interactions in assembly of the bacteriorhodopsin lattice
    • Isenbarger, T. A., and M. P. Krebs. 1999. Role of helix-helix interactions in assembly of the bacteriorhodopsin lattice. Biochemistry. 38:9023-9030.
    • (1999) Biochemistry , vol.38 , pp. 9023-9030
    • Isenbarger, T.A.1    Krebs, M.P.2
  • 80
    • 21244472381 scopus 로고    scopus 로고
    • Can the low-resolution structures of photointermediates of bacteriorhodopsin explain their crystal structures?
    • Kamikubo, H., and M. Kataoka. 2005. Can the low-resolution structures of photointermediates of bacteriorhodopsin explain their crystal structures? Biophys. J. 88:1925-1931.
    • (2005) Biophys. J , vol.88 , pp. 1925-1931
    • Kamikubo, H.1    Kataoka, M.2
  • 81
    • 0024962341 scopus 로고
    • Bacteriorhodopsin mutants of Halobacterium sp. GRB II. Characterization of mutants
    • Soppa, J., J. Otomo, J. Straub, J. Tittor, S. Messen, and D. Oesterhelt. 1989. Bacteriorhodopsin mutants of Halobacterium sp. GRB II. Characterization of mutants. J. Biol. Chem. 264:13049-13056.
    • (1989) J. Biol. Chem , vol.264 , pp. 13049-13056
    • Soppa, J.1    Otomo, J.2    Straub, J.3    Tittor, J.4    Messen, S.5    Oesterhelt, D.6
  • 82
    • 0141817701 scopus 로고    scopus 로고
    • The discovery of the α-helix and β-sheet, the principal structural features of proteins
    • Eisenberg, D. 2003. The discovery of the α-helix and β-sheet, the principal structural features of proteins. Proc. Natl. Acad. Sci. USA. 100:11207-11210.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11207-11210
    • Eisenberg, D.1
  • 83
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller, D. J., A. Engel, and M. Amrein. 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    Engel, A.2    Amrein, M.3


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