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Volumn 281, Issue 4, 1998, Pages 587-592

Assessing the functionality of a membrane protein in a three-dimensional crystal

Author keywords

Bacteriorhodopsin; FT IR; Lipidic cubic phase crystallization; Proton transfer; Time resolved

Indexed keywords

BACTERIORHODOPSIN; LIPID; MEMBRANE PROTEIN;

EID: 0032575766     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1970     Document Type: Article
Times cited : (50)

References (24)
  • 3
    • 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
  • 4
    • 0000593842 scopus 로고
    • FTIR studies on crystals of photosynthetic reaction centers
    • Gerwert K., Hess B., Michel H., Buchanan S. FTIR studies on crystals of photosynthetic reaction centers. FEBS Letters. 232:1988;303-307
    • (1988) FEBS Letters , vol.232 , pp. 303-307
    • Gerwert, K.1    Hess, B.2    Michel, H.3    Buchanan, S.4
  • 6
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
    • Haupts U., Tittor J., Bamberg E., Oesterhelt D. General concept for ion translocation by halobacterial retinal proteins The isomerization/switch/transfer (IST) model. Biochemistry. 36:1997;2-7
    • (1997) Biochemistry , vol.36 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 7
    • 0030134661 scopus 로고    scopus 로고
    • ATR/FT-IR difference spectroscopy of biological matter with microsecond time resolution
    • Heberle J., Zscherp C. ATR/FT-IR difference spectroscopy of biological matter with microsecond time resolution. Appl. Spectrosc. 50:1996;588-596
    • (1996) Appl. Spectrosc. , vol.50 , pp. 588-596
    • Heberle, J.1    Zscherp, C.2
  • 8
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N.T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:1975;28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 9
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • 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 cryomicroscopy. 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
  • 11
    • 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., Büldt G. Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10:1991;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
  • 12
    • 0027526352 scopus 로고
    • Mechanism of light-dependent proton translocation by bacteriorhodopsin
    • Krebs M.P., Khorana H.G. Mechanism of light-dependent proton translocation by bacteriorhodopsin. J. Bacteriol. 175:1993;1555-1560
    • (1993) J. Bacteriol. , vol.175 , pp. 1555-1560
    • Krebs, M.P.1    Khorana, H.G.2
  • 13
    • 0030703429 scopus 로고    scopus 로고
    • The adsorption of paraquat on silver electrode surfaces: A SERS microprobe study
    • Kreisig S., Tarazona A., Koglin E. The adsorption of paraquat on silver electrode surfaces a SERS microprobe study. Electrochim. Acta. 42:1997;3335-3344
    • (1997) Electrochim. Acta , vol.42 , pp. 3335-3344
    • Kreisig, S.1    Tarazona, A.2    Koglin, E.3
  • 14
    • 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
  • 15
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi J.K. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta. 1183:1993;241-261
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 17
    • 85005500629 scopus 로고
    • Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin
    • Maeda A. Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin. Israel J. Chem. 35:1995;387-400
    • (1995) Israel J. Chem. , vol.35 , pp. 387-400
    • Maeda, A.1
  • 18
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Ångstroms 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 Ångstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 19
    • 0025868156 scopus 로고
    • Fourier transform infrared study of the N intermediate of bacteriorhodopsin
    • Pfefferlé J.-M., Maeda A., Sasaki J., Yoshizawa T. Fourier transform infrared study of the N intermediate of bacteriorhodopsin. Biochemistry. 30:1991;6548-6556
    • (1991) Biochemistry , vol.30 , pp. 6548-6556
    • Pfefferlé, J.-M.1    Maeda, A.2    Sasaki, J.3    Yoshizawa, T.4
  • 20
    • 33845377796 scopus 로고
    • Theoretical studies of proton transfer
    • Scheiner S. Theoretical studies of proton transfer. Acc. Chem. Res. 18:1985;174-180
    • (1985) Acc. Chem. Res. , vol.18 , pp. 174-180
    • Scheiner, S.1
  • 21
    • 0025834125 scopus 로고
    • Chromophore motion during the bacteriorhodopsin photocycle: Polarized absorption spectroscopy of bacteriorhodopsin and ist M-state in bacteriorhodopsin crystals
    • Schertler G.F.X., Lozier R., Michel H., Oesterhelt D. Chromophore motion during the bacteriorhodopsin photocycle polarized absorption spectroscopy of bacteriorhodopsin and ist M-state in bacteriorhodopsin crystals. EMBO J. 10:1991;2353-2361
    • (1991) EMBO J. , vol.10 , pp. 2353-2361
    • Schertler, G.F.X.1    Lozier, R.2    Michel, H.3    Oesterhelt, D.4
  • 22
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert F. Infrared spectroscopy applied to biochemical and biological problems. Methods Enzymol. 246:1995;501-526
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 23
    • 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
  • 24
    • 0031553201 scopus 로고    scopus 로고
    • Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy
    • Zscherp C., Heberle J. Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy. J. Phys. Chem. 101:1997;10542-10547
    • (1997) J. Phys. Chem. , vol.101 , pp. 10542-10547
    • Zscherp, C.1    Heberle, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.