메뉴 건너뛰기




Volumn 287, Issue 1, 1999, Pages 145-161

Protein conformational changes in the bacteriorhodopsin photocycle

Author keywords

Conformational change; Electron crystallography; Proton pump; Seven helix membrane protein; Trapped intermediates

Indexed keywords

BACTERIORHODOPSIN; ETHANE; MUTANT PROTEIN;

EID: 0033582945     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2589     Document Type: Article
Times cited : (235)

References (61)
  • 1
    • 0025299602 scopus 로고
    • The role of back-reactions and proton uptake during the N→O transition in bacteriorhodopsin's photocycle: A kinetic resonance Raman study
    • Ames J. B., Mathies R. A. The role of back-reactions and proton uptake during the N→O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study. Biochemistry. 29:1990;7181-7190.
    • (1990) Biochemistry , vol.29 , pp. 7181-7190
    • Ames, J.B.1    Mathies, R.A.2
  • 2
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J., Henderson R. Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy. 14:1984;319-336.
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.1    Henderson, R.2
  • 3
    • 0023803129 scopus 로고
    • Controlled environment vitrification system: An improved sample preparation technique
    • Bellare J., Davis H. T., Scriven L. E., Talmon Y. Controlled environment vitrification system: An improved sample preparation technique. J. Electr. Micros. Techn. 10:1988;87-111.
    • (1988) J. Electr. Micros. Techn. , vol.10 , pp. 87-111
    • Bellare, J.1    Davis, H.T.2    Scriven, L.E.3    Talmon, Y.4
  • 4
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryomicroscopy combined with rapid mixing of spray droplets
    • Berriman J., Unwin N. Analysis of transient structures by cryomicroscopy combined with rapid mixing of spray droplets. Ultramicroscopy. 56:1994;241-252.
    • (1994) Ultramicroscopy , vol.56 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 5
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M and N-photointermediates
    • Braiman M. S., Bousche O., Rothschild K. J. Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M and N-photointermediates. Proc. Natl Acad. Sci. USA. 88:1991;2388-2392.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2388-2392
    • Braiman, M.S.1    Bousche, O.2    Rothschild, K.J.3
  • 6
    • 0028239690 scopus 로고
    • The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues
    • Brown L. S., Yamazaki Y., Maeda A., Sun L., Needleman R., Lanyi J. K. The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues. J. Mol. Biol. 239:1994a;401-414.
    • (1994) J. Mol. Biol. , vol.239 , pp. 401-414
    • Brown, L.S.1    Yamazaki, Y.2    Maeda, A.3    Sun, L.4    Needleman, R.5    Lanyi, J.K.6
  • 8
    • 0033548544 scopus 로고    scopus 로고
    • The projection structure of the K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction
    • Bullough P., Henderson R. The projection structure of the K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction. J. Mol. Biol. 286:1999;1661-1669.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1661-1669
    • Bullough, P.1    Henderson, R.2
  • 9
    • 0344335730 scopus 로고
    • Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump
    • Butt H. J., Fendler K., Bamberg E., Tittor J., Oesterhelt D. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J. 8:1989;1657-1663.
    • (1989) EMBO J. , vol.8 , pp. 1657-1663
    • Butt, H.J.1    Fendler, K.2    Bamberg, E.3    Tittor, J.4    Oesterhelt, D.5
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. Jackson. Boca Raton: CRC Press
    • Ebrey T. G. Light energy transduction in bacteriorhodopsin. Jackson M. Thermodynamics of Membrane Receptors and Channels. 1993;353-387 CRC Press, Boca Raton.
    • (1993) Thermodynamics of Membrane Receptors and Channels , pp. 353-387
    • Ebrey, T.G.1
  • 15
    • 0027536538 scopus 로고
    • Homologous bacterio-opsin encoding gene expression via site-specific vector integration
    • Ferrando E., Schweiger U., Oesterhelt D. Homologous bacterio-opsin encoding gene expression via site-specific vector integration. Gene. 125:1993;41-47.
    • (1993) Gene , vol.125 , pp. 41-47
    • Ferrando, E.1    Schweiger, U.2    Oesterhelt, D.3
  • 17
  • 19
    • 0001652299 scopus 로고
    • Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin
    • Grzesiek S., Dencher N. A. Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin. FEBS Letters. 208:1986;337-342.
    • (1986) FEBS Letters , vol.208 , pp. 337-342
    • Grzesiek, S.1    Dencher, N.A.2
  • 20
    • 0031684846 scopus 로고    scopus 로고
    • Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle
    • Hendrickson F. M., Burkard F., Glaeser R. M. Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle. Biophys. J. 75:1998;1446-1454.
    • (1998) Biophys. J. , vol.75 , pp. 1446-1454
    • Hendrickson, F.M.1    Burkard, F.2    Glaeser, R.M.3
  • 23
    • 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
  • 24
    • 70149124337 scopus 로고    scopus 로고
    • Polarized FTIR spectroscopy distinguishes peptide backbone changes in the M and N photointermediates of bacteriorhodopsin
    • Kandori H. Polarized FTIR spectroscopy distinguishes peptide backbone changes in the M and N photointermediates of bacteriorhodopsin. J. Am. Chem. Soc. 120:1998;4546-4547.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4546-4547
    • Kandori, H.1
  • 25
    • 0030904207 scopus 로고    scopus 로고
    • Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin
    • Kandori H., Yamazaki Y., Hatanaka M., Needleman R., Brown L. S., Richter H. T., Lanyi J. K., Maeda A. Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin. Biochemistry. 36:1997;5134-5141.
    • (1997) Biochemistry , vol.36 , pp. 5134-5141
    • Kandori, H.1    Yamazaki, Y.2    Hatanaka, M.3    Needleman, R.4    Brown, L.S.5    Richter, H.T.6    Lanyi, J.K.7    Maeda, A.8
  • 27
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch M. H. J., Dencher N., 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.2    Oesterhelt, D.3    Plöhn, H.-J.4    Rapp, G.5    Büldt, G.6
  • 28
    • 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
  • 29
    • 0031470604 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin D85N/D96N double mutant showing substantial structural changes and a highly twinned, disordered lattice
    • Lindahl M., Henderson R. Structure of the bacteriorhodopsin D85N/D96N double mutant showing substantial structural changes and a highly twinned, disordered lattice. Ultramicroscopy. 70:1998;95-106.
    • (1998) Ultramicroscopy , vol.70 , pp. 95-106
    • Lindahl, M.1    Henderson, R.2
  • 30
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium Halobium
    • Lozier R. H., Bogomolni R. A., Stoeckenius W. Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium. Biophys. J. 15:1975;955-963.
    • (1975) Biophys. J. , vol.15 , pp. 955-963
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 31
    • 0030612782 scopus 로고    scopus 로고
    • Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light-driven proton transport
    • Ludlam G. J., Rothschild K. J. Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light-driven proton transport. FEBS Letters. 407:1997;285-288.
    • (1997) FEBS Letters , vol.407 , pp. 285-288
    • Ludlam, G.J.1    Rothschild, K.J.2
  • 32
    • 0001710879 scopus 로고
    • Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin
    • Marinetti T., Subramaniam S., Mogi T., Marti T., Khorana H. G. Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin. Proc. Natl Acad. Sci. USA. 86:1989;529-533.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 529-533
    • Marinetti, T.1    Subramaniam, S.2    Mogi, T.3    Marti, T.4    Khorana, H.G.5
  • 33
    • 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., 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.4    Heyn, M.P.5    Khorana, H.G.6
  • 34
    • 0026926972 scopus 로고
    • Limits of cryofixation as seen by Fourier transform infrared spectra of metmyoglobin azide and carbonyl hemoglobin in vitrified and freeze concentrated aqueous solution
    • Mayer E., Astl G. Limits of cryofixation as seen by Fourier transform infrared spectra of metmyoglobin azide and carbonyl hemoglobin in vitrified and freeze concentrated aqueous solution. Ultramicroscopy. 45:1992;185-197.
    • (1992) Ultramicroscopy , vol.45 , pp. 185-197
    • Mayer, E.1    Astl, G.2
  • 35
    • 0025011266 scopus 로고
    • Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor
    • Miller A., Oesterhelt D. Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor. Biochim. Biophys. Acta. 1020:1990;57-64.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 57-64
    • Miller, A.1    Oesterhelt, D.2
  • 36
    • 0016376428 scopus 로고
    • Isolation of cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D., Stoeckenius W. Isolation of cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:1974;667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 37
    • 0026623260 scopus 로고
    • A unifying concept for ion translocation by retinal proteins
    • Oesterhelt D., Tittor J., Bamberg E. A unifying concept for ion translocation by retinal proteins. J. Bioenerg. Biomemb. 24:1992;181-191.
    • (1992) J. Bioenerg. Biomemb. , vol.24 , pp. 181-191
    • Oesterhelt, D.1    Tittor, J.2    Bamberg, E.3
  • 38
    • 0024317089 scopus 로고
    • Aspartic acid 96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto H., Mareti T., Holz M., Mogi T., Lindau M., Khorana H. G., Heyn M. P. Aspartic acid 96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl Acad. Sci. USA. 86:1989;9228-9232.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Mareti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 39
    • 0025016817 scopus 로고
    • Substitution of amino acids Asp-85, Asp-212 and Arg-82 in bacteriorhodopsin affects the proton release of the pump and the pK of the Schiff base
    • Otto H., Mareti 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 of the pump and the pK 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    Mareti, T.2    Holz, M.3    Mogi, T.4    Stern, L.J.5    Engel, F.6    Khorana, H.G.7    Heyn, M.P.8
  • 40
    • 0025868156 scopus 로고
    • Fourier Transform infrared study of the N intermediate of bacteriorhodopsin
    • Pfefferle J.-M., Maeda A., Sasaki J., Yoshizawa Y. Fourier Transform infrared study of the N intermediate of bacteriorhodopsin. Biochemistry. 30:1991;6548-6556.
    • (1991) Biochemistry , vol.30 , pp. 6548-6556
    • Pfefferle, J.-M.1    Maeda, A.2    Sasaki, J.3    Yoshizawa, Y.4
  • 41
    • 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
  • 42
    • 0030010796 scopus 로고    scopus 로고
    • D38 is an essential part of the proton translocation pathway in bacteriorhodopsin
    • Riesle J., Oesterhelt D., Dencher N., Heberle J. D38 is an essential part of the proton translocation pathway in bacteriorhodopsin. Biochemistry. 35:1996;6635-6643.
    • (1996) Biochemistry , vol.35 , pp. 6635-6643
    • Riesle, J.1    Oesterhelt, D.2    Dencher, N.3    Heberle, J.4
  • 44
    • 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
  • 46
    • 0017879924 scopus 로고
    • A mechanism for the light-driven proton pump of Halobacterium halobium
    • Schulten K., Tavan P. A mechanism for the light-driven proton pump of Halobacterium halobium. Nature. 272:1978;85-86.
    • (1978) Nature , vol.272 , pp. 85-86
    • Schulten, K.1    Tavan, P.2
  • 48
    • 0026746612 scopus 로고
    • Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy
    • Souvignier G., Gerwert K. Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy. Biophys. J. 63:1992;1393-1405.
    • (1992) Biophys. J. , vol.63 , pp. 1393-1405
    • Souvignier, G.1    Gerwert, K.2
  • 51
    • 0025157075 scopus 로고
    • Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg82→Ala and Asp85→Glu: The blue form is inactive in proton translocation
    • Subramaniam S., Marti T., Khorana H. G. Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg82→Ala and Asp85→Glu: the blue form is inactive in proton translocation. Proc. Natl Acad. Sci. USA. 87:1990;1013-1017.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 52
    • 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
  • 53
    • 0031042723 scopus 로고    scopus 로고
    • Electron diffraction studies of light-induced conformational changes in the Leu-93→Ala bacteriorhodopsin mutant
    • Subramaniam S., Faruqi A. R., Oesterhelt D., Henderson R. Electron diffraction studies of light-induced conformational changes in the Leu-93→Ala bacteriorhodopsin mutant. Proc. Natl Acad. Sci. USA. 94:1997;1767-1772.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1767-1772
    • Subramaniam, S.1    Faruqi, A.R.2    Oesterhelt, D.3    Henderson, R.4
  • 55
    • 0024325044 scopus 로고
    • A defective proton pump, point-mutated bacteriorhodopsin Asp 96→Asn is fully re-activated by azide
    • Tittor J., Soell C., Oesterhelt D., Butt H.-J., Bamberg E. A defective proton pump, point-mutated bacteriorhodopsin Asp 96→Asn is fully re-activated by azide. EMBO J. 8:1989;3477-3482.
    • (1989) EMBO J. , vol.8 , pp. 3477-3482
    • Tittor, J.1    Soell, C.2    Oesterhelt, D.3    Butt, H.-J.4    Bamberg, E.5
  • 56
    • 0019302483 scopus 로고
    • Light isomerizes the chromophore of bacteriorhodopsin
    • Tsuda M., Glaccum M., Nelson B., Ebrey T. G. Light isomerizes the chromophore of bacteriorhodopsin. Nature. 287:1980;351-353.
    • (1980) Nature , vol.287 , pp. 351-353
    • Tsuda, M.1    Glaccum, M.2    Nelson, B.3    Ebrey, T.G.4
  • 57
    • 0025871066 scopus 로고
    • Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle
    • Varo G., Lanyi J. K. Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biochemistry. 30:1991a;5008-5015.
    • (1991) Biochemistry , vol.30 , pp. 5008-5015
    • Varo, G.1    Lanyi, J.K.2
  • 58
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Varo G., Lanyi J. K. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry. 30:1991b;5016-5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Varo, G.1    Lanyi, J.K.2
  • 59
    • 0029886089 scopus 로고    scopus 로고
    • A 3-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 3-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
  • 60
    • 0032579445 scopus 로고    scopus 로고
    • Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction
    • Weik M., Zaccai G., Dencher N. A., Oesterhelt D. Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction. J. Mol. Biol. 275:1998;625-634.
    • (1998) J. Mol. Biol. , vol.275 , pp. 625-634
    • Weik, M.1    Zaccai, G.2    Dencher, N.A.3    Oesterhelt, D.4
  • 61
    • 0031880854 scopus 로고    scopus 로고
    • A computer-controlled spraying-freezing apparatus for millisecond time-resolution electron cryo-microscopy
    • White H. D., Walker M. L., Trinick J. A computer-controlled spraying-freezing apparatus for millisecond time-resolution electron cryo-microscopy. J. Struct. Biol. 121:1998;306-313.
    • (1998) J. Struct. Biol. , vol.121 , pp. 306-313
    • White, H.D.1    Walker, M.L.2    Trinick, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.