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Volumn 291, Issue 4, 1999, Pages 899-911

Structure of bacteriorhodopsin at 1.55 Å resolution

Author keywords

Bacteriorhodopsin; Hydrogen bonded chain; Membrane proteins; Proton pump; X ray crystallography

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; LYSINE; MEMBRANE PROTEIN; PROLINE; SCHIFF BASE;

EID: 0033609904     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3027     Document Type: Article
Times cited : (1336)

References (60)
  • 1
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov S. P., Imasheva E. S., Govindjee R., Ebrey T. G. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70:1996;473-481.
    • (1996) Biophys. J. , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 2
    • 0027244529 scopus 로고
    • Estimated acid dissociation constants of the Schiff base, Asp-85 and Arg-82 during the bacteriorhodopsin photocycle
    • Brown L. S., Bonet L., Needleman R., Lanyi J. K. Estimated acid dissociation constants of the Schiff base, Asp-85 and Arg-82 during the bacteriorhodopsin photocycle. Biophys. J. 65:1993;124-130.
    • (1993) Biophys. J. , vol.65 , pp. 124-130
    • Brown, L.S.1    Bonet, L.2    Needleman, R.3    Lanyi, J.K.4
  • 3
    • 0028787636 scopus 로고
    • Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle
    • Brown L. S., Váró G., Needleman R., Lanyi J. K. Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle. Biophys. J. 69:1995;2103-2111.
    • (1995) Biophys. J. , vol.69 , pp. 2103-2111
    • Brown, L.S.1    Váró, G.2    Needleman, R.3    Lanyi, J.K.4
  • 4
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate 96 to the bacteriorhodopsin Schiff base
    • Cao Y., Váró G., Chang M., Ni B., Needleman R., Lanyi J. K. Water is required for proton transfer from aspartate 96 to the bacteriorhodopsin Schiff base. Biochemistry. 30:1991;10972-10979.
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Váró, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 7
    • 0028793135 scopus 로고
    • Molecular mechanism of protein-retinal coupling in bacteriorhodopsin
    • Delaney J. K., Schweiger U., Subramaniam S. Molecular mechanism of protein-retinal coupling in bacteriorhodopsin. Proc. Natl Acad. Sci. USA. 92:1995;11120-11124.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11120-11124
    • Delaney, J.K.1    Schweiger, U.2    Subramaniam, S.3
  • 8
    • 0018793025 scopus 로고
    • Bacteriorhodopsin monomers pump protons
    • Dencher N. A., Heyn M. P. Bacteriorhodopsin monomers pump protons. FEBS Letters. 108:1979;307-310.
    • (1979) FEBS Letters , vol.108 , pp. 307-310
    • Dencher, N.A.1    Heyn, M.P.2
  • 9
    • 0024744871 scopus 로고
    • Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
    • Dencher N. A., Dresselhaus D., Zaccai G., Büldt G. Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl Acad. Sci. USA. 86:1989;7876-7879.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Büldt, G.4
  • 10
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • Dioumaev A. K., Richter H. T., Brown L. S., Tanio M., Tuzi S., Saitô H., Kimura Y., Needleman R., Lanyi J. K. Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry. 37:1998;2496-2506.
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saitô, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 11
    • 0029968737 scopus 로고    scopus 로고
    • Chemical and functional studies on the importance of purple membrane lipids in bacteriorhodopsin photocycle behavior
    • Dracheva S., Bose S., Hendler R. W. Chemical and functional studies on the importance of purple membrane lipids in bacteriorhodopsin photocycle behavior. FEBS Letters. 382:1996;209-212.
    • (1996) FEBS Letters , vol.382 , pp. 209-212
    • Dracheva, S.1    Bose, S.2    Hendler, R.W.3
  • 12
    • 0029960813 scopus 로고    scopus 로고
    • Detailed description of an alpha helix→pi bulge transition detected by molecular dynamics simulations of the p185c-erbB2 V659G transmembrane domain
    • Duneau J. P., Genest D., Genest M. Detailed description of an alpha helix→pi bulge transition detected by molecular dynamics simulations of the p185c-erbB2 V659G transmembrane domain. J. Biomol. Struc. Dynam. 13:1996;753-769.
    • (1996) J. Biomol. Struc. Dynam. , vol.13 , pp. 753-769
    • Duneau, J.P.1    Genest, D.2    Genest, M.3
  • 13
    • 0023040477 scopus 로고
    • Orientation of bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy
    • Earnest T. N., Roepe P., Braiman M. S., Gillespie J., Rothschild K. J. Orientation of bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy. Biochemistry. 25:1986;7793-7798.
    • (1986) Biochemistry , vol.25 , pp. 7793-7798
    • Earnest, T.N.1    Roepe, P.2    Braiman, M.S.3    Gillespie, J.4    Rothschild, K.J.5
  • 14
    • 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., Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl Acad. Sci. USA. 95:1998;11673-11678.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 15
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D. L., Altenbach C., Yang K., Hubbell W. L., Khorana H. G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science. 274:1996;768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 17
    • 0028093220 scopus 로고
    • The bacteriorhodopsin photocycle: Direct structural study of two substates of the M-intermediate
    • Han B.-G., Vonck J., Glaeser R. M. The bacteriorhodopsin photocycle: direct structural study of two substates of the M-intermediate. Biophys. J. 67:1994;1179-1186.
    • (1994) Biophys. J. , vol.67 , pp. 1179-1186
    • Han, B.-G.1    Vonck, J.2    Glaeser, R.M.3
  • 18
    • 0030840715 scopus 로고    scopus 로고
    • Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy
    • Hatanaka M., Kandori H., Maeda A. Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy. Biophys. J. 73:1997;1001-1006.
    • (1997) Biophys. J. , vol.73 , pp. 1001-1006
    • Hatanaka, M.1    Kandori, H.2    Maeda, A.3
  • 19
    • 0032575766 scopus 로고    scopus 로고
    • Assessing the functionality of a membrane protein in a three-dimensional crystal
    • Heberle J., Büldt G., Koglin E., Rosenbusch J. P., Landau E. M. Assessing the functionality of a membrane protein in a three-dimensional crystal. J. Mol. Biol. 281:1998;587-592.
    • (1998) J. Mol. Biol. , vol.281 , pp. 587-592
    • Heberle, J.1    Büldt, G.2    Koglin, E.3    Rosenbusch, J.P.4    Landau, E.M.5
  • 20
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 21
  • 22
    • 0028016119 scopus 로고
    • Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs
    • Ihara K., Amemiya T., Miyashita Y., Mukohata Y. Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs. Biophys. J. 67:1994;1187-1191.
    • (1994) Biophys. J. , vol.67 , pp. 1187-1191
    • Ihara, K.1    Amemiya, T.2    Miyashita, Y.3    Mukohata, Y.4
  • 23
    • 0028890031 scopus 로고
    • Structure at 2. 8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2. 8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 25
    • 0032514725 scopus 로고    scopus 로고
    • Importance of specific native lipids in controlling the photocycle of bacteriorhodopsin
    • Joshi M. K., Dracheva S., Mukhopadhyay A. K., Bose S., Hendler R. W. Importance of specific native lipids in controlling the photocycle of bacteriorhodopsin. Biochemistry. 37:1998;14463-14470.
    • (1998) Biochemistry , vol.37 , pp. 14463-14470
    • Joshi, M.K.1    Dracheva, S.2    Mukhopadhyay, A.K.3    Bose, S.4    Hendler, R.W.5
  • 27
    • 0030813030 scopus 로고    scopus 로고
    • The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration
    • Kamikubo H., Oka T., Imamoto Y., Tokunaga F., Lanyi J. K., Kataoka M. The last phase of the reprotonation switch in bacteriorhodopsin: the transition between the M-type and the N-type protein conformation depends on hydration. Biochemistry. 36:1997;12282-12287.
    • (1997) Biochemistry , vol.36 , pp. 12282-12287
    • Kamikubo, H.1    Oka, T.2    Imamoto, Y.3    Tokunaga, F.4    Lanyi, J.K.5    Kataoka, M.6
  • 29
    • 21244499919 scopus 로고
    • Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
    • Kates M., Kushwaha S. C., Sprott G. D. Lipids of purple membrane from extreme halophiles and of methanogenic bacteria. Methods Enzymol. 88:1982;98-111.
    • (1982) Methods Enzymol. , vol.88 , pp. 98-111
    • Kates, M.1    Kushwaha, S.C.2    Sprott, G.D.3
  • 30
    • 0027467033 scopus 로고
    • The alpha aneurism: A structural motif revealed in an insertion mutant of staphylococcal nuclease
    • Keefe L. J., Sondek J., Shortle D., Lattman E. E. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc. Natl Acad. Sci. USA. 90:1993;3275-3279.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3275-3279
    • Keefe, L.J.1    Sondek, J.2    Shortle, D.3    Lattman, E.E.4
  • 32
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau E. M., Rosenbusch J. P. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA. 93:1996;14532-14535.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 33
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi J. K. Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272:1997;31209-31212.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 34
    • 0024741970 scopus 로고
    • Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism
    • Lin S. W., Mathies R. A. Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism. Biophys. J. 56:1989;653-660.
    • (1989) Biophys. J. , vol.56 , pp. 653-660
    • Lin, S.W.1    Mathies, R.A.2
  • 35
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 Å resolution
    • Luecke H., Richter H. T., Lanyi J. K. Proton transfer pathways in bacteriorhodopsin at 2.3 Å resolution. Science. 280:1998;1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 36
    • 0028279038 scopus 로고
    • Interaction of aspartate 85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: A Fourier transform infrared spectroscopy study
    • Maeda A., Sasaki J., Yamazaki Y., Needleman R., Lanyi J. K. Interaction of aspartate 85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier transform infrared spectroscopy study. Biochemistry. 33:1994;1713-1717.
    • (1994) Biochemistry , vol.33 , pp. 1713-1717
    • Maeda, A.1    Sasaki, J.2    Yamazaki, Y.3    Needleman, R.4    Lanyi, J.K.5
  • 37
    • 0025873898 scopus 로고
    • Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
    • Marti T., Otto H., Mogi T., Rösselet S. J., Heyn M. P., Khorana H. G. Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation. J. Biol. Chem. 266:1991;6919-6927.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6919-6927
    • Marti, T.1    Otto, H.2    Mogi, T.3    Rösselet, S.J.4    Heyn, M.P.5    Khorana, H.G.6
  • 38
    • 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., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., Fujiyoshi Y. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol. 286:1999;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
  • 39
    • 0026319199 scopus 로고
    • Protein folding association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 40
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8:1998;489-500.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 41
    • 0025016817 scopus 로고
    • Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the p K of the Schiff base
    • Otto H., Marti T., Holz M., Mogi T., Stern L. J., Engel F., Khorana H. G., Heyn M. P. Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the p K of the Schiff base. Proc. Natl Acad. Sci. USA. 87:1990;1018-1022.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1018-1022
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Stern, L.J.5    Engel, F.6    Khorana, H.G.7    Heyn, M.P.8
  • 43
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J. P., Landau E. M. X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. Science. 277:1997;676-1681.
    • (1997) Science , vol.277 , pp. 676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 44
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
    • Rammelsberg R., Huhn G., Lübben M., Gerwert K. Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network. Biochemistry. 37:1998;5001-5009.
    • (1998) Biochemistry , vol.37 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lübben, M.3    Gerwert, K.4
  • 45
    • 0029665673 scopus 로고    scopus 로고
    • a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:1996;4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 46
    • 0030901231 scopus 로고    scopus 로고
    • The tertiary structural changes in bacteriorhodopsin occur between M states; X-ray diffraction and Fourier transform infrared spectroscopy
    • Sass H. J., Schachowa I. W., Rapp G., Koch M. H. J., Oesterhelt D., Dencher N. A., Büldt G. The tertiary structural changes in bacteriorhodopsin occur between M states; X-ray diffraction and Fourier transform infrared spectroscopy. EMBO J. 16:1997;1484-1491.
    • (1997) EMBO J. , vol.16 , pp. 1484-1491
    • Sass, H.J.1    Schachowa, I.W.2    Rapp, G.3    Koch, M.H.J.4    Oesterhelt, D.5    Dencher, N.A.6    Büldt, G.7
  • 49
    • 0027967379 scopus 로고
    • Protein-protein interaction converts a proton pump into a sensory receptor
    • Spudich J. L. Protein-protein interaction converts a proton pump into a sensory receptor. Cell. 79:1994;747-750.
    • (1994) Cell , vol.79 , pp. 747-750
    • Spudich, J.L.1
  • 50
    • 0031000202 scopus 로고    scopus 로고
    • Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base Asp-73 interhelical salt bridge
    • Spudich E. N., Zhang W. S., Alam M., Spudich J. L. Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base Asp-73 interhelical salt bridge. Proc. Natl Acad. Sci. USA. 94:1997;4960-4965.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4960-4965
    • Spudich, E.N.1    Zhang, W.S.2    Alam, M.3    Spudich, J.L.4
  • 51
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S., Gerstein M., Oesterhelt D., Henderson R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12:1993;1-8.
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 52
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • Takeda K., Sato H., Hino T., Kono M., Fukuda K., Sakurai I., Okada T., Kouyama T. A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J. Mol. Biol. 283:1998;463-474.
    • (1998) J. Mol. Biol. , vol.283 , pp. 463-474
    • Takeda, K.1    Sato, H.2    Hino, T.3    Kono, M.4    Fukuda, K.5    Sakurai, I.6    Okada, T.7    Kouyama, T.8
  • 55
    • 0030065552 scopus 로고    scopus 로고
    • Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle
    • Váró G., Needleman R., Lanyi J. K. Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle. Biophys. J. 70:1996;461-467.
    • (1996) Biophys. J. , vol.70 , pp. 461-467
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 56
    • 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. 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. 35:1996;5870-5878.
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 57
    • 0029738907 scopus 로고    scopus 로고
    • Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 13- cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle
    • Weidlich O., Schalt B., Friedman N., Sheves M., Lanyi J. K., Brown L. S., Siebert F. Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 13- cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle. Biochemistry. 35:1996;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
  • 58
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White S. H., Wimley W. C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:1999;319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 60
    • 0033514438 scopus 로고    scopus 로고
    • The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices
    • Zhang X. N., Zhu J. Y., Spudich J. L. The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices. Proc. Natl Acad. Sci. USA. 96:1999;857-862.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 857-862
    • Zhang, X.N.1    Zhu, J.Y.2    Spudich, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.