메뉴 건너뛰기




Volumn 31, Issue 7, 2002, Pages 539-548

Two processes lead to a stable all-trans and 13-cis isomer equilibrium in dark-adapted bacteriorhodopsin; effect of high pressure on bacteriorhodopsin, bacteriorhodopsin mutant D96N and fluoro-bacteriorhodopsin analogues

Author keywords

Bacteriorhodopsin analogues; Dark adapted bacteriorhodopsin; High pressure; Molar volume changes

Indexed keywords

10 FLUORO BACTERIORHODOPSIN; 12 FLUORO BACTERIORHODOPSIN; 14 FLUORO BACTERIORHODOPSIN; ASPARTIC ACID; BACTERIORHODOPSIN; FLUORINE DERIVATIVE; FUNCTIONAL GROUP; MUTANT PROTEIN; SCHIFF BASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0036972618     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-002-0250-2     Document Type: Article
Times cited : (12)

References (60)
  • 1
    • 0026651047 scopus 로고
    • C13 NMR studies of model compounds for bacteriorhodopsin: Facts affecting the retinal chromophore chemical-shift and absorption maximum
    • Albeck A, Livanah N, Gottlieb H, Sheves M (1992) C13 NMR studies of model compounds for bacteriorhodopsin: facts affecting the retinal chromophore chemical-shift and absorption maximum. J Am Chem Soc 114:2400-2411
    • (1992) J Am Chem Soc , vol.114 , pp. 2400-2411
    • Albeck, A.1    Livanah, N.2    Gottlieb, H.3    Sheves, M.4
  • 2
    • 0000185399 scopus 로고
    • The preparation of vicinal difluoroolefinic carbonyl compounds and their application to the synthesis of difluororetinal analogs
    • Asato AE, Liu RSH (1986) The preparation of vicinal difluoroolefinic carbonyl compounds and their application to the synthesis of difluororetinal analogs. Tetrahedron Lett 27: 3337-3340
    • (1986) Tetrahedron Lett , vol.27 , pp. 3337-3340
    • Asato, A.E.1    Liu, R.S.H.2
  • 3
    • 33947093371 scopus 로고
    • Fluorinated rhodopsin analogues from 10-fluoro- and 14-fluororetinal
    • Asato AE, Matsumoto H, Denny M, Liu RSH (1978) Fluorinated rhodopsin analogues from 10-fluoro- and 14-fluororetinal. J Am Chem Soc 100:5957-5960
    • (1978) J Am Chem Soc , vol.100 , pp. 5957-5960
    • Asato, A.E.1    Matsumoto, H.2    Denny, M.3    Liu, R.S.H.4
  • 6
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it is says about chromophore isomerization and proton release
    • Balashov SP, Imasheva ES, Govindjee R, Ebrey TG (1996) Titration of aspartate-85 in bacteriorhodopsin: what it is says about chromophore isomerization and proton release. Biophys J 70:473-481
    • (1996) Biophys J , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 7
    • 0017146723 scopus 로고
    • Effects of light adaptation on the purple membrane structure of Halobacterium halobium
    • Becher B, Cassim JY (1976) Effects of light adaptation on the purple membrane structure of Halobacterium halobium. Biophys J 16:1183-1200
    • (1976) Biophys J , vol.16 , pp. 1183-1200
    • Becher, B.1    Cassim, J.Y.2
  • 9
    • 0035114879 scopus 로고    scopus 로고
    • The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles
    • Bryl K, Yoshihara K (2001) The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles. Eur Biophys J 29:628-640
    • (2001) Eur Biophys J , vol.29 , pp. 628-640
    • Bryl, K.1    Yoshihara, K.2
  • 10
    • 0026714325 scopus 로고
    • Unique biphasic band shape of the visible circular dichroism of bacteriorhodopsin in purple membrane. Excitions, multiple transitions or protein heterogeneity?
    • Cassim JY (1992) Unique biphasic band shape of the visible circular dichroism of bacteriorhodopsin in purple membrane. Excitions, multiple transitions or protein heterogeneity? Biophys J 63:1432-1442
    • (1992) Biophys J , vol.63 , pp. 1432-1442
    • Cassim, J.Y.1
  • 11
    • 0025775579 scopus 로고
    • O-H stretching vibration in Fourier transform difference infrared spectra of bacteriorhodopsin
    • Chang C-W, Sekiya N, Yoshihara K (1991) O-H stretching vibration in Fourier transform difference infrared spectra of bacteriorhodopsin. FEBS Lett 287:157-159
    • (1991) FEBS Lett , vol.287 , pp. 157-159
    • Chang, C.-W.1    Sekiya, N.2    Yoshihara, K.3
  • 12
    • 0022847386 scopus 로고
    • Studies of rhodopsin and bacteriorhodopsin using modified retinals
    • Crouch R (1986) Studies of rhodopsin and bacteriorhodopsin using modified retinals. Photochem Photobiol 44:803-807
    • (1986) Photochem Photobiol , vol.44 , pp. 803-807
    • Crouch, R.1
  • 13
    • 0020540613 scopus 로고
    • Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments
    • Dencher NA, Kohl K-D, Heyn MP (1983) Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments. Biochemistry 22:1323-1334
    • (1983) Biochemistry , vol.22 , pp. 1323-1334
    • Dencher, N.A.1    Kohl, K.-D.2    Heyn, M.P.3
  • 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 WD, Oesterhelt D (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.-O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 15
    • 0012966233 scopus 로고
    • Photocurrent of dark-adapted bacteriorhodopsin
    • Fahr A, Bamberg E (1982) Photocurrent of dark-adapted bacteriorhodopsin. FEBS Lett 140:251-253
    • (1982) FEBS Lett , vol.140 , pp. 251-253
    • Fahr, A.1    Bamberg, E.2
  • 17
    • 0030894962 scopus 로고    scopus 로고
    • Interaction between Asp-85 and the proton-releasing group in bacteriorhodospin. A study of an O-like photocycle intermediate
    • Gat Y, Friedman N, Sheves M, Ottolenghi M (1997) Interaction between Asp-85 and the proton-releasing group in bacteriorhodospin. A study of an O-like photocycle intermediate. Biochemistry 36:4135-4148
    • (1997) Biochemistry , vol.36 , pp. 4135-4148
    • Gat, Y.1    Friedman, N.2    Sheves, M.3    Ottolenghi, M.4
  • 18
    • 0034681198 scopus 로고    scopus 로고
    • Structural investigation of the active site in bacteriorhodopsin: Geometric constrains on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR
    • Griffiths JM, Bennett AE, Engelhard M, Siebert F, Raap J, Lugtenburg J, Herzfeld J, Griffin RG (2000) Structural investigation of the active site in bacteriorhodopsin: geometric constrains on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR. Biochemistry 39:362-371
    • (2000) Biochemistry , vol.39 , pp. 362-371
    • Griffiths, J.M.1    Bennett, A.E.2    Engelhard, M.3    Siebert, F.4    Raap, J.5    Lugtenburg, J.6    Herzfeld, J.7    Griffin, R.G.8
  • 20
    • 0028220701 scopus 로고
    • Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M, Jaenicke R (1994) Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 221:617-630
    • (1994) Eur J Biochem , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 22
    • 0027249907 scopus 로고
    • Decoupling of photoand proton cycle in the Asp85→Glu mutant of bacteriorhodopsin
    • Heberle J, Oesterhelt D, Dencher NA (1993) Decoupling of photoand proton cycle in the Asp85→Glu mutant of bacteriorhodopsin. EMBO J 12:3721-3727
    • (1993) EMBO J , vol.12 , pp. 3721-3727
    • Heberle, J.1    Oesterhelt, D.2    Dencher, N.A.3
  • 23
    • 0034702811 scopus 로고    scopus 로고
    • Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhodopsin by heteronuclear solid-state NMR distance measurements
    • Helmle M, Petzelt H, Ockenfels A, Gartner W, Oesterhelt D, Bechinger B (2000) Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhodopsin by heteronuclear solid-state NMR distance measurements. Biochemistry 39:10066-10071
    • (2000) Biochemistry , vol.39 , pp. 10066-10071
    • Helmle, M.1    Petzelt, H.2    Ockenfels, A.3    Gartner, W.4    Oesterhelt, D.5    Bechinger, B.6
  • 24
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213:899-929
    • (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
  • 25
    • 0028258544 scopus 로고
    • Molecular dynamics study of bacteriorhodopsin and artificial pigments
    • Humphrey W, Logunov I, Schulten K, Sheves M (1994) Molecular dynamics study of bacteriorhodopsin and artificial pigments. Biochemistry 33:3668-3678
    • (1994) Biochemistry , vol.33 , pp. 3668-3678
    • Humphrey, W.1    Logunov, I.2    Schulten, K.3    Sheves, M.4
  • 26
    • 0017389861 scopus 로고
    • On the photocycle and light adaptation of dark-adapted bacteriorhodopsin
    • Kalisky O, Goldschmidt CHR, Ottolenghi M (1977) On the photocycle and light adaptation of dark-adapted bacteriorhodopsin. Biophys J 19:185-189
    • (1977) Biophys J , vol.19 , pp. 185-189
    • Kalisky, O.1    Goldschmidt, C.H.R.2    Ottolenghi, M.3
  • 28
    • 0001445637 scopus 로고
    • Partial molar volumes of arbitrary shape and the effect of hydrogen bonding with water
    • Kharakoz DP (1992) Partial molar volumes of arbitrary shape and the effect of hydrogen bonding with water. J Solution Chem 21:569-595
    • (1992) J Solution Chem , vol.21 , pp. 569-595
    • Kharakoz, D.P.1
  • 29
    • 0344936736 scopus 로고    scopus 로고
    • The chromophore induces a correct folding of the polypeptide chain of bacteriorhodopsin
    • Kollbach G, Steinmuller S, Berndsen T, Buss V, Gartner W (1998) The chromophore induces a correct folding of the polypeptide chain of bacteriorhodopsin. Biochemistry 37:8227-8232
    • (1998) Biochemistry , vol.37 , pp. 8227-8232
    • Kollbach, G.1    Steinmuller, S.2    Berndsen, T.3    Buss, V.4    Gartner, W.5
  • 30
    • 0027278014 scopus 로고
    • Pressure effects on the dark-adaptation of bacteriorhodopsin
    • Kovacs I, Nienhaus GU, Philipp R, Xie A (1993) Pressure effects on the dark-adaptation of bacteriorhodopsin. Biophys J 64:1187-1193
    • (1993) Biophys J , vol.64 , pp. 1187-1193
    • Kovacs, I.1    Nienhaus, G.U.2    Philipp, R.3    Xie, A.4
  • 31
    • 84961983828 scopus 로고    scopus 로고
    • Quantum chemistry: Molecular dynamics study of the dark-adaptation process in bacteriorhodopsin
    • Logunov I, Schulten K (1996) Quantum chemistry: molecular dynamics study of the dark-adaptation process in bacteriorhodopsin. J Am Chem Soc 118:9727-9735
    • (1996) J Am Chem Soc , vol.118 , pp. 9727-9735
    • Logunov, I.1    Schulten, K.2
  • 33
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke H, Richter H-T, Lanyi JK (1998) Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280:1934-1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 35
    • 0017699799 scopus 로고
    • Isomeric composition of retinal chromophore in dark-adapted bacteriorhodopsin
    • Maeda A, Iwasa T, Yoshizawa T (1977) Isomeric composition of retinal chromophore in dark-adapted bacteriorhodopsin. J Biochem (Tokyo) 82:1599-1604.
    • (1977) J Biochem (Tokyo) , vol.82 , pp. 1599-1604
    • Maeda, A.1    Iwasa, T.2    Yoshizawa, T.3
  • 36
    • 0030968284 scopus 로고    scopus 로고
    • Investigation of the proton release channel of bacteriorhodopsin in different intermediates of the photo cycle. A molecular dynamics study
    • Nagel J, Edholm O, Berger O, Jähnig F (1997) Investigation of the proton release channel of bacteriorhodopsin in different intermediates of the photo cycle. A molecular dynamics study. Biochemistry 36:2875-2883
    • (1997) Biochemistry , vol.36 , pp. 2875-2883
    • Nagel, J.1    Edholm, O.2    Berger, O.3    Jähnig, F.4
  • 37
    • 0000748473 scopus 로고
    • Pressure dependence of weak acid ionization in aqueous buffers
    • Neuman RC, Kauzmann W, Zipp A (1973) Pressure dependence of weak acid ionization in aqueous buffers. J Phys Chem 22:2687-2691
    • (1973) J Phys Chem , vol.22 , pp. 2687-2691
    • Neuman, R.C.1    Kauzmann, W.2    Zipp, A.3
  • 38
    • 0000585345 scopus 로고
    • Resonance Raman spectra of 13-demethylretinal bacteriorhodopsin and of a picosecond bathochromic photocycle intermediate
    • Noguchi T, Kolaczkowski S, Gartner W, Atkinson GH (1990) Resonance Raman spectra of 13-demethylretinal bacteriorhodopsin and of a picosecond bathochromic photocycle intermediate. J Phys Chem 94:4920-4926
    • (1990) J Phys Chem , vol.94 , pp. 4920-4926
    • Noguchi, T.1    Kolaczkowski, S.2    Gartner, W.3    Atkinson, G.H.4
  • 39
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of the retinal proteins from halophilic archaea
    • Oesterhelt D (1998) The structure and mechanism of the family of the retinal proteins from halophilic archaea. Curr Opin Struct Biol 8:489-500
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 41
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase
    • Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM (1997) X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase. 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
  • 43
    • 0030010796 scopus 로고    scopus 로고
    • D38 is an essential part of the proton translocation pathway in bacteriorhodopsin
    • Riesle J, Oesterhelt D, Dencher NA, Heberle J (1996) D38 is an essential part of the proton translocation pathway in bacteriorhodopsin. Biochemistry 35:6635-6643
    • (1996) Biochemistry , vol.35 , pp. 6635-6643
    • Riesle, J.1    Oesterhelt, D.2    Dencher, N.A.3    Heberle, J.4
  • 45
    • 0030913277 scopus 로고    scopus 로고
    • Threonine-89 participates in the active site of bacteriorhodopsin: Evidence for a role in color regulation and Schiff base proton transfer
    • Russel T, Coleman M, Rath P, Nilsson A, Rothschild KJ (1997) Threonine-89 participates in the active site of bacteriorhodopsin: evidence for a role in color regulation and Schiff base proton transfer. Biochemistry 36:7490-7497
    • (1997) Biochemistry , vol.36 , pp. 7490-7497
    • Russel, T.1    Coleman, M.2    Rath, P.3    Nilsson, A.4    Rothschild, K.J.5
  • 46
    • 0024977340 scopus 로고
    • Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomers
    • Scherrer P, Mathew MK, Sperling W, Stoeckenius W (1989) Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomers. Biochemistry 28:829-834
    • (1989) Biochemistry , vol.28 , pp. 829-834
    • Scherrer, P.1    Mathew, M.K.2    Sperling, W.3    Stoeckenius, W.4
  • 47
    • 0028980597 scopus 로고
    • High-pressure near-infrared Raman spectroscopy of bacteriorhodopsin light to dark adaptation
    • Schulte A, Bradley IIL (1995) High-pressure near-infrared Raman spectroscopy of bacteriorhodopsin light to dark adaptation. Biophys J 69:1554-1562
    • (1995) Biophys J , vol.69 , pp. 1554-1562
    • Schulte, A.1    Bradley, I.I.L.2
  • 48
    • 0012906653 scopus 로고
    • Equilibrium composition of retinal isomers in dark-dapted bacteriorhodopsin and effect of high pressure probed by near-infrared Raman spectroscopy
    • Schulte A, Bradley IIL, Williams C (1995) Equilibrium composition of retinal isomers in dark-dapted bacteriorhodopsin and effect of high pressure probed by near-infrared Raman spectroscopy. Appl Spectrosc 49:80-83
    • (1995) Appl Spectrosc , vol.49 , pp. 80-83
    • Schulte, A.1    Bradley, I.I.L.2    Williams, C.3
  • 49
    • 0026530231 scopus 로고
    • Solvent isotope effects on retinal cis-trans isomerization in the dark adaptation of bacteriorhodopsin
    • Seltzer S (1992) Solvent isotope effects on retinal cis-trans isomerization in the dark adaptation of bacteriorhodopsin. J Am Chem Soc 114:3516-3520
    • (1992) J Am Chem Soc , vol.114 , pp. 3516-3520
    • Seltzer, S.1
  • 50
    • 0021744582 scopus 로고
    • Factors affecting the rate of the thermal isomerization of 13-cis-bacteriorhodopsin to all-trans
    • Sheves M, Baasov T (1984) Factors affecting the rate of the thermal isomerization of 13-cis-bacteriorhodopsin to all-trans. J Am Chem Soc 106:6840-6841
    • (1984) J Am Chem Soc , vol.106 , pp. 6840-6841
    • Sheves, M.1    Baasov, T.2
  • 51
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • Smith SO, Pardoen JA, Lugtenburg J, Mathies RA (1987) Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin. J Phys Chem 91:804-819
    • (1987) J Phys Chem , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 52
    • 0024982103 scopus 로고
    • Structure and protein environment of the retinal chromophore in light- and dark-adapted bacteriorhodopsin studied by solid-state NMR
    • Smith SO, de Groot HJM, Gebhard R, Courtin JML, Lugtenburg J, Herzfeld J, Griffin RG (1989) Structure and protein environment of the retinal chromophore in light- and dark-adapted bacteriorhodopsin studied by solid-state NMR. Biochemistry 28:8897-8904
    • (1989) Biochemistry , vol.28 , pp. 8897-8904
    • Smith, S.O.1    De Groot, H.J.M.2    Gebhard, R.3    Courtin, J.M.L.4    Lugtenburg, J.5    Herzfeld, J.6    Griffin, R.G.7
  • 53
    • 0024962341 scopus 로고
    • Bacteriorhodopsin mutants of Halobacterium sp. GRB. II. Characterization of mutants
    • Soppa J, Otomo J, Straub J, Tittor J, Meeszen S, Oesterhelt D (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    Meeszen, S.5    Oesterhelt, D.6
  • 54
    • 0017714656 scopus 로고
    • Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers
    • Sperling W, Carl P, Pafferty ChN, Dencher NA (1977) Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers. Biophys Struct Mechanism 3:79-94
    • (1977) Biophys Struct Mechanism , vol.3 , pp. 79-94
    • Sperling, W.1    Carl, P.2    Pafferty, Ch.N.3    Dencher, N.A.4
  • 55
    • 84989742241 scopus 로고
    • Isomer composition and spectra of the dark and light adapted forms of artificial becteriorhodopsins
    • Steinberg G, Friedman N, Sheves M, Ottolenghi M (1991) Isomer composition and spectra of the dark and light adapted forms of artificial becteriorhodopsins. Photochem Photobiol 54:969-976
    • (1991) Photochem Photobiol , vol.54 , pp. 969-976
    • Steinberg, G.1    Friedman, N.2    Sheves, M.3    Ottolenghi, M.4
  • 57
    • 0023115506 scopus 로고
    • Rapid charge separation and batochromic absorption shift of flash-excited bacteriorhodopsin containing 13-cis or all-trans forms of substituted retinals
    • Trissl H-W, Gartner W (1987) Rapid charge separation and batochromic absorption shift of flash-excited bacteriorhodopsin containing 13-cis or all-trans forms of substituted retinals. Biochemistry 26:751-758
    • (1987) Biochemistry , vol.26 , pp. 751-758
    • Trissl, H.-W.1    Gartner, W.2
  • 58
    • 0018881176 scopus 로고
    • Effect of high pressure on the absorption spectrum and isomeric composition of bacteriorhodopsin
    • Tsuda M, Ebrey TG (1980) Effect of high pressure on the absorption spectrum and isomeric composition of bacteriorhodopsin. Biophys J 30:149-158
    • (1980) Biophys J , vol.30 , pp. 149-158
    • Tsuda, M.1    Ebrey, T.G.2
  • 59
    • 21844513082 scopus 로고
    • Picosecond resonance coherent anti-Stokes Raman spectroscopy of bacteriorhodopsin: Quantitative third-order susceptibility analysis of the dark-adapted mixture
    • Ujj L, Popp A, Atkinson GH (1994) Picosecond resonance coherent anti-Stokes Raman spectroscopy of bacteriorhodopsin: quantitative third-order susceptibility analysis of the dark-adapted mixture. Chem Phys 188:221-234
    • (1994) Chem Phys , vol.188 , pp. 221-234
    • Ujj, L.1    Popp, A.2    Atkinson, G.H.3
  • 60
    • 0012966235 scopus 로고
    • Light- and dark-adaptation of bacteriorhodopsin measured by a photoelectric method
    • Varo G, Bryl K (1988) Light- and dark-adaptation of bacteriorhodopsin measured by a photoelectric method. Biochim Biophys Acta 934:247-252
    • (1988) Biochim Biophys Acta , vol.934 , pp. 247-252
    • Varo, G.1    Bryl, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.