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Volumn 44, Issue 11, 2005, Pages 4572-4581

Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation

Author keywords

[No Author keywords available]

Indexed keywords

CENTRIFUGATION; DIMERS; GEL PERMEATION CHROMATOGRAPHY; LIGHT SCATTERING; PLANTS (BOTANY); PROTEINS; SIZE DETERMINATION; SYNCHROTRON RADIATION;

EID: 15544386013     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047685q     Document Type: Article
Times cited : (34)

References (67)
  • 1
    • 0032568601 scopus 로고    scopus 로고
    • The nature of the excited state of the reaction center of photosystem II of green plants: A high-resolution fluorescence spectroscopy study
    • Peterman, E. J. G., van Amerongen, H., van Grondelle, R., and Dekker, J. P. (1998) The nature of the excited state of the reaction center of photosystem II of green plants: A high-resolution fluorescence spectroscopy study, Proc. Natl. Acad. Sci. U.S.A. 95, 6128-6133.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6128-6133
    • Peterman, E.J.G.1    Van Amerongen, H.2    Van Grondelle, R.3    Dekker, J.P.4
  • 2
    • 0037417876 scopus 로고    scopus 로고
    • A quantitative structure-function relationship for the photosystem II reaction center: Supermolecular behavior in natural photosynthesis
    • Barter, L. M., Durrant, J. R., and Klug, D. R. (2003) A quantitative structure-function relationship for the photosystem II reaction center: Supermolecular behavior in natural photosynthesis, Proc. Natl. Acad. Sci. U.S.A. 100, 946-951.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 946-951
    • Barter, L.M.1    Durrant, J.R.2    Klug, D.R.3
  • 3
    • 0035808704 scopus 로고    scopus 로고
    • Photosynthetic water oxidation to molecular oxygen: Apparatus and mechanism
    • Renger, G. (2001) Photosynthetic water oxidation to molecular oxygen: apparatus and mechanism, Biochim. Biophys. Acta 1503, 210-228.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 210-228
    • Renger, G.1
  • 4
    • 0037295369 scopus 로고    scopus 로고
    • Photosystem II: The engine of life
    • Barber, J. (2003) Photosystem II: the engine of life, Q. Rev. Biophys. 36, 71-89.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 71-89
    • Barber, J.1
  • 6
    • 11144285975 scopus 로고    scopus 로고
    • Preparation, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus
    • Kern, J., Loll, B., Lüneberg, C., DiFiore, D., Biesiadka, J., Irrgang, K.-D., and Zouni, A. (2005) Preparation, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus, Biochim. Biophys. Acta, 1706, 147-157.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 147-157
    • Kern, J.1    Loll, B.2    Lüneberg, C.3    Difiore, D.4    Biesiadka, J.5    Irrgang, K.-D.6    Zouni, A.7
  • 7
    • 0001505435 scopus 로고
    • Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559
    • Nanba, O., and Satoh, K. (1987) Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559, Proc. Natl. Acad. Sci. U.S.A. 84, 109-112.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 109-112
    • Nanba, O.1    Satoh, K.2
  • 8
    • 0000125543 scopus 로고
    • Isolation and characterisation of D1/D2/cytochrome b559 complex from Synechocystis 6803
    • Gounaris, K., Chapman, D. J., and Barber, J. (1989) Isolation and characterisation of D1/D2/cytochrome b559 complex from Synechocystis 6803, Biochim. Biophys. Acta 973, 296-301.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 296-301
    • Gounaris, K.1    Chapman, D.J.2    Barber, J.3
  • 9
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of Photosystem II
    • Seidler, A. (1996) The extrinsic polypeptides of Photosystem II, Biochim. Biophys. Acta 1277, 35-60.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 10
    • 15544385845 scopus 로고    scopus 로고
    • Subunit composition of Photosystem II Core Complexes from the cyanobacterium Thermosynechococcus elongatus and the higher plant Spinacia oleracea
    • submittted
    • Kern, J., Zouni, A., Franke, P., Schröder, W., and Irrgang, K.-D. (2004) Subunit composition of Photosystem II Core Complexes from the cyanobacterium Thermosynechococcus elongatus and the higher plant Spinacia oleracea, Plant J., submittted.
    • (2004) Plant J.
    • Kern, J.1    Zouni, A.2    Franke, P.3    Schröder, W.4    Irrgang, K.-D.5
  • 11
    • 1042290470 scopus 로고    scopus 로고
    • The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
    • Shi, L. X., and Schröder, W. P. (2004) The low molecular mass subunits of the photosynthetic supracomplex, photosystem II, Biochim. Biophys. Acta 1608, 75-96.
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 75-96
    • Shi, L.X.1    Schröder, W.P.2
  • 12
    • 0025195358 scopus 로고
    • Functional and structural analysis of photosystem II core complexes from spinach with high oxygen evolution capacity
    • Haag, E., Irrgang, K.-D., Boekema, E. J., and Renger, G. (1990) Functional and structural analysis of photosystem II core complexes from spinach with high oxygen evolution capacity, Eur. J. Biochem. 189, 47-53.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 47-53
    • Haag, E.1    Irrgang, K.-D.2    Boekema, E.J.3    Renger, G.4
  • 13
    • 0000433293 scopus 로고
    • Size, Shape and mass of the oxygen-evolving photosystem II complex from the thermophilic cyanobacterium Synechococcus sp
    • Rögner, M., Dekker, J. P., Boekema, E. J., and Wilt, H. T. (1987) Size, Shape and mass of the oxygen-evolving photosystem II complex from the thermophilic cyanobacterium Synechococcus sp., FEBS Lett. 219, 207-211.
    • (1987) FEBS Lett. , vol.219 , pp. 207-211
    • Rögner, M.1    Dekker, J.P.2    Boekema, E.J.3    Wilt, H.T.4
  • 14
    • 0025747903 scopus 로고
    • Density determination by analytical ultracentrifugation in a rapid dynamical gradient: Application to lipid and detergent aggregates containing proteins
    • Lustig, A., Engel, A., and Zulauf, M. (1991) Density determination by analytical ultracentrifugation in a rapid dynamical gradient: application to lipid and detergent aggregates containing proteins, Biochim. Biophys. Acta 1115, 89-95.
    • (1991) Biochim. Biophys. Acta , vol.1115 , pp. 89-95
    • Lustig, A.1    Engel, A.2    Zulauf, M.3
  • 16
    • 0029141507 scopus 로고
    • Photosystem II 3-D structure and the role of the extrinsic subunits in photosynthetic oxygen evolution
    • Ford, R. C., Rosenberg, M. F., Shepherd, F. H., McPhie, P., and Holzenburg, A. (1995) Photosystem II 3-D structure and the role of the extrinsic subunits in photosynthetic oxygen evolution, Micron 26, 133-140.
    • (1995) Micron , vol.26 , pp. 133-140
    • Ford, R.C.1    Rosenberg, M.F.2    Shepherd, F.H.3    McPhie, P.4    Holzenburg, A.5
  • 18
  • 19
    • 0027169050 scopus 로고
    • Formation and characterization of two-dimensional crystals of photosystem II
    • Lyon, M. K., Marr, K. M., and Furcinitti, P. S. (1993) Formation and characterization of two-dimensional crystals of photosystem II, J. Struct. Biol. 110, 133-140.
    • (1993) J. Struct. Biol. , vol.110 , pp. 133-140
    • Lyon, M.K.1    Marr, K.M.2    Furcinitti, P.S.3
  • 20
    • 0028346592 scopus 로고
    • Three-dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo
    • Santini, C., Tidu, V., Tognon, G., Ghiretti Magaldi, A., and Bassi, R. (1994) Three-dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo, Eur. J. Biochem. 221, 307-315.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 307-315
    • Santini, C.1    Tidu, V.2    Tognon, G.3    Ghiretti Magaldi, A.4    Bassi, R.5
  • 22
    • 0029670059 scopus 로고    scopus 로고
    • Two-dimensional crystals of photosystem II: Biochemical characterization, cryoelectron microscopy and localization of the D1 and cytochrome b559 polypeptides
    • Marr, K. M., Mastronarde, D. N., and Lyon, M. K. (1996) Two-dimensional crystals of photosystem II: biochemical characterization, cryoelectron microscopy and localization of the D1 and cytochrome b559 polypeptides, J. Cell Biol. 132, 823-833.
    • (1996) J. Cell Biol. , vol.132 , pp. 823-833
    • Marr, K.M.1    Mastronarde, D.N.2    Lyon, M.K.3
  • 23
    • 0034730964 scopus 로고    scopus 로고
    • Supermolecular structure of photosystem II and location of the PsbS protein
    • Nield, J., Funk, C., and Barber, J. (2000) Supermolecular structure of photosystem II and location of the PsbS protein, Philos. Trans. R. Soc. London, Ser. B: Biol. Sci. 355, 1337-1344.
    • (2000) Philos. Trans. R. Soc. London, Ser. B: Biol. Sci. , vol.355 , pp. 1337-1344
    • Nield, J.1    Funk, C.2    Barber, J.3
  • 24
    • 0035210531 scopus 로고    scopus 로고
    • Supermolecular organization of photosystem II and its associated light harvesting antenna in Arabidopsis thaliana
    • Yakushevska, A. E., Jensen, P. E., Keegstra, W., van Roon, H., Scheller, H. V., Boekema, E. J., and Dekker, J. P. (2001) Supermolecular organization of photosystem II and its associated light harvesting antenna in Arabidopsis thaliana, Eur. J. Biochem. 268, 6020-6028.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6020-6028
    • Yakushevska, A.E.1    Jensen, P.E.2    Keegstra, W.3    Van Roon, H.4    Scheller, H.V.5    Boekema, E.J.6    Dekker, J.P.7
  • 25
    • 0034617209 scopus 로고    scopus 로고
    • Towards structural determination of the water-splitting enzyme. Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium
    • Kuhl, H., Kruip, J., Seidler, A., Krieger-Liszkay, A., Bunker, M., Bald, D., Scheidig, A. J., and Rögner, M. (2000) Towards structural determination of the water-splitting enzyme. Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium, J. Biol. Chem. 275, 20652-20659.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20652-20659
    • Kuhl, H.1    Kruip, J.2    Seidler, A.3    Krieger-Liszkay, A.4    Bunker, M.5    Bald, D.6    Scheidig, A.J.7    Rögner, M.8
  • 26
    • 0034610351 scopus 로고    scopus 로고
    • Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus
    • Shen, J. R., and Kamiya, N. (2000) Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus, Biochemistry 39, 14739-14744.
    • (2000) Biochemistry , vol.39 , pp. 14739-14744
    • Shen, J.R.1    Kamiya, N.2
  • 27
    • 0030426392 scopus 로고    scopus 로고
    • Progress towards structural elucidation of Photosystem II
    • Tsiotis, G., McDermott, G., and Ghanotakis, D. (1996) Progress towards structural elucidation of Photosystem II, Photosynth. Res. 50, 93-101.
    • (1996) Photosynth. Res. , vol.50 , pp. 93-101
    • Tsiotis, G.1    McDermott, G.2    Ghanotakis, D.3
  • 28
    • 0005861896 scopus 로고    scopus 로고
    • Polypeptides of Photosystem II
    • (Singhal, G. S., Renger, G., Sopory, S. K., Irrgang, K.-D., Govindjee, Eds.), Narosa Publishing House, New Dehli, India
    • Ghanotakis, D. F., Tsiotis, G., and Bricker, T. M. (1999) Polypeptides of Photosystem II, in Concepts in Photobiology: Photosynthesis and Photomorphogenesis (Singhal, G. S., Renger, G., Sopory, S. K., Irrgang, K.-D., Govindjee, Eds.) pp 264-291, Narosa Publishing House, New Dehli, India.
    • (1999) Concepts in Photobiology: Photosynthesis and Photomorphogenesis , pp. 264-291
    • Ghanotakis, D.F.1    Tsiotis, G.2    Bricker, T.M.3
  • 30
    • 0003058264 scopus 로고
    • Extraction and characterisation of oxygen-evolving Photosystem II complexes from a thermophilic cyanobacterium Synechococcus spec
    • Schatz, G. H., and Witt, H. T. (1984) Extraction and characterisation of oxygen-evolving Photosystem II complexes from a thermophilic cyanobacterium Synechococcus spec., Photobiochem. Photobiophys. 7, 1-14.
    • (1984) Photobiochem. Photobiophys. , vol.7 , pp. 1-14
    • Schatz, G.H.1    Witt, H.T.2
  • 31
    • 0032311408 scopus 로고    scopus 로고
    • Improved isolation and crystallization of photosystem I for structural analysis
    • Fromme, P., and Witt, H. T. (1998) Improved isolation and crystallization of photosystem I for structural analysis, Biochim. Biophys. Acta 1365, 175-184.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 175-184
    • Fromme, P.1    Witt, H.T.2
  • 32
    • 0028956304 scopus 로고
    • Photosystem I from Synechococcus elongatus: Preparation and crystallization of monomers with varying subunit compositions
    • Jekow, P., Fromme, P., Witt, H. T., and Saenger, W. (1995) Photosystem I from Synechococcus elongatus: preparation and crystallization of monomers with varying subunit compositions, Biochim. Biophys. Acta 1229, 115-120.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 115-120
    • Jekow, P.1    Fromme, P.2    Witt, H.T.3    Saenger, W.4
  • 33
    • 0024351273 scopus 로고
    • Isolation and characterization of the Ch1 a/b protein complex CP29 from spinach
    • Henrysson, T., Schröder, W. P., Åkerlund, H.-E., and Spangfort, M. (1989) Isolation and characterization of the Ch1 a/b protein complex CP29 from spinach, Biochim. Biophys. Acta 977, 301-308.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 301-308
    • Henrysson, T.1    Schröder, W.P.2    Åkerlund, H.-E.3    Spangfort, M.4
  • 35
    • 1842427662 scopus 로고    scopus 로고
    • Fluorescence decay kinetics of solubilized pigment protein complexes from the distal, proximal, and core antenna of photosystem II in the range of 10-277 K and absence or presence of sucrose
    • Huyer, J., Eckert, H.-J., Eichler, H. J., Irrgang, K.-D., Miao, J., and Renger, G. (2004) Fluorescence Decay Kinetics of Solubilized Pigment Protein Complexes from the Distal, Proximal, and Core Antenna of Photosystem II in the Range of 10-277 K and Absence or Presence of Sucrose, J. Phys. Chem. B 108, 3326-3334.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3326-3334
    • Huyer, J.1    Eckert, H.-J.2    Eichler, H.J.3    Irrgang, K.-D.4    Miao, J.5    Renger, G.6
  • 36
    • 0024248215 scopus 로고
    • Structural determination of the photosystem II core complex from spinach
    • Irrgang, K.-D., Boekema, E. J., Vater, J., and Renger, G. (1988) Structural determination of the photosystem II core complex from spinach, Eur. J. Biochem. 178, 209-217.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 209-217
    • Irrgang, K.-D.1    Boekema, E.J.2    Vater, J.3    Renger, G.4
  • 37
    • 0030901810 scopus 로고    scopus 로고
    • Quenching of chlorophyll a fluorescence in the aggregates of LHCII: Steady-state fluorescence and picosecond relaxation kinetics
    • Vasil'ev, S., Irrgang, K.-D., Schrötter, T., Bergmann, A., Eichler, H. J., and Renger, G. (1997) Quenching of chlorophyll a fluorescence in the aggregates of LHCII: steady-state fluorescence and picosecond relaxation kinetics, Biochemistry 36, 7503-7512.
    • (1997) Biochemistry , vol.36 , pp. 7503-7512
    • VasiL'Ev, S.1    Irrgang, K.-D.2    Schrötter, T.3    Bergmann, A.4    Eichler, H.J.5    Renger, G.6
  • 38
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous-equations for assaying chlorophyll a and chlorophyll b extracted with 4 different solvents-verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R. J., Thompson, W. A., and Kriedemann, P. E. (1989) Determination of accurate extinction coefficients and simultaneous-equations for assaying chlorophyll a and chlorophyll b extracted with 4 different solvents-verification of the concentration of chlorophyll standards by atomic absorption spectroscopy, Biochim. Biophys. Acta 975, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 39
    • 8144227878 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.2 Å resolution: A closer look at the Mn-cluster
    • Biesiadka, J., Loll, B., Kern, J., Irrgang, K.-D., and Zouni, A. (2004) Crystal structure of cyanobacterial photosystem II at 3.2 Å resolution: a closer look at the Mn-cluster, Phys. Chem. Chem. Phys. 6, 4733-4736.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4733-4736
    • Biesiadka, J.1    Loll, B.2    Kern, J.3    Irrgang, K.-D.4    Zouni, A.5
  • 40
    • 0001218414 scopus 로고
    • The Use of Cyanobacteria in the Study of the Structure and Function of Photosystem II
    • (Bryant, D. A., Ed.), Kluwer Academic Publishers, Dordrecht, Netherlands
    • Barry, B. A., Boerner, R. J., and de Paula, L. C. (1994) The Use of Cyanobacteria in the Study of the Structure and Function of Photosystem II, in The Molecular Biology of Cyanobacteria (Bryant, D. A., Ed.) pp 217-257, Kluwer Academic Publishers, Dordrecht, Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 217-257
    • Barry, B.A.1    Boerner, R.J.2    De Paula, L.C.3
  • 41
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P., Fromme, P., Witt, H. T., Klukas, O., Saenger, W., and Krauss, N. (2001) Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution, Nature 411, 909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 42
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: Elimination of interfering substances
    • Brown, R. E., Jarvin, K. L., and Hyland, K. J. (1989) Protein measurement using bicinchoninic acid: elimination of interfering substances, Anal. Biochem. 180, 136-139.
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvin, K.L.2    Hyland, K.J.3
  • 43
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu, Z., Yan, H., Wang, K., Kuang, T., Zhang, J., Gui, L., An, X., and Chang, W. (2004) Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution, Nature 428, 287-292.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 44
    • 0019328971 scopus 로고
    • Alkyl glycoside detergents: A simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase
    • Rosevear, P., VanAken, T., Baxter, J., and Ferguson-Miller, S. (1980) Alkyl glycoside detergents: a simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase, Biochemistry 19, 4108-4115.
    • (1980) Biochemistry , vol.19 , pp. 4108-4115
    • Rosevear, P.1    Vanaken, T.2    Baxter, J.3    Ferguson-Miller, S.4
  • 45
    • 15544365238 scopus 로고
    • Über einige Erfahrungen mit der digitalen Dichtemesseinrichtung DMA 10 zur Bestimmung des partiellen spezifischen Volumens von Haemoglobin
    • Behlke, J. (1971) Über einige Erfahrungen mit der digitalen Dichtemesseinrichtung DMA 10 zur Bestimmung des partiellen spezifischen Volumens von Haemoglobin, Stud. Biophys. 28.
    • (1971) Stud. Biophys. , vol.28
    • Behlke, J.1
  • 46
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic of integral equations
    • Provencher, S. W. (1982) A constrained regularization method for inverting data represented by linear algebraic of integral equations, Comput. Phys. Commun. 27, 213-228.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-228
    • Provencher, S.W.1
  • 47
    • 0020176708 scopus 로고
    • CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations
    • Provencher, S. W. (1982) CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations, Comput. Phys. Commun. 27, 229-242.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 229-242
    • Provencher, S.W.1
  • 48
    • 0030995661 scopus 로고    scopus 로고
    • Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
    • Behlke, J., Ristau, O., and Schonfeld, H. J. (1997) Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions, Biochemistry 36, 5149-5156.
    • (1997) Biochemistry , vol.36 , pp. 5149-5156
    • Behlke, J.1    Ristau, O.2    Schonfeld, H.J.3
  • 49
    • 0033401728 scopus 로고    scopus 로고
    • Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43
    • Sugiura, M., and Inoue, Y. (1999) Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43, Plant Cell Physiol. 40, 1219-1231.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2
  • 50
    • 0019464240 scopus 로고
    • Physical studies on the ribosomal protein-S2 from the Escherichia coli 30S subunit
    • Georgalis, Y., Giri, L., and Littlechild, J. A. (1981) Physical studies on the ribosomal protein-S2 from the Escherichia coli 30S subunit, Biochemistry 20, 1061-1064.
    • (1981) Biochemistry , vol.20 , pp. 1061-1064
    • Georgalis, Y.1    Giri, L.2    Littlechild, J.A.3
  • 51
    • 0028196887 scopus 로고
    • Light scattering by bovine alpha-crystallin proteins in solution: Hydrodynamic structure and interparticle interaction
    • Xia, J. Z., Aerts, T., Donceel, K., and Clauwaert, J. (1994) Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction, Biophys. J. 66, 861-872.
    • (1994) Biophys. J. , vol.66 , pp. 861-872
    • Xia, J.Z.1    Aerts, T.2    Donceel, K.3    Clauwaert, J.4
  • 53
    • 0000498521 scopus 로고
    • Concentration dependence of the diffusion coefficient of a dimerizing Protein: Bovine pancreatic trypsin inhibitor
    • Wills, P. R., and Georgalis, Y. (1981) Concentration dependence of the diffusion coefficient of a dimerizing Protein: Bovine pancreatic trypsin inhibitor, J. Phys. Chem. 85, 3978-3983.
    • (1981) J. Phys. Chem. , vol.85 , pp. 3978-3983
    • Wills, P.R.1    Georgalis, Y.2
  • 54
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules-theory and applications
    • de la Torre, G. J., and Bloomfield, V. A. (1981) Hydrodynamic properties of complex, rigid, biological macromolecules-theory and applications, Q. Rev. Biophys. 14, 81-139.
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • Torre, G.J.1    Bloomfield, V.A.2
  • 55
    • 84933517499 scopus 로고
    • Variational treatment of hydrodynamic interaction in polymers
    • Rotne, J., and Prager, S. (1969) Variational treatment of hydrodynamic interaction in polymers, J. Chem. Phys. 50, 4831-4837.
    • (1969) J. Chem. Phys. , vol.50 , pp. 4831-4837
    • Rotne, J.1    Prager, S.2
  • 56
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz, Y., Gerstein, M., and Chothia, C. (1994) Volume changes on protein folding, Structure 2, 641-649.
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 57
    • 0034607357 scopus 로고    scopus 로고
    • Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle
    • Lustig, A., Engel, A., Tsiotis, G., Landau, E. M., and Baschong, W. (2000) Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle, Biochim. Biophys. Acta 1464, 199-206.
    • (2000) Biochim. Biophys. Acta , vol.1464 , pp. 199-206
    • Lustig, A.1    Engel, A.2    Tsiotis, G.3    Landau, E.M.4    Baschong, W.5
  • 58
    • 0000922351 scopus 로고
    • Influence of polydispersity on protein crystallization: A quasi-elastic light-scattering study applied to α-amylase
    • Veesler, S., Marq, S., Lafont, S., Astier, J. P., and Boistelle, R. P. (1994) Influence of polydispersity on protein crystallization: a quasi-elastic light-scattering study applied to α-amylase, Acta Crystallogr. D50, 355-360.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 355-360
    • Veesler, S.1    Marq, S.2    Lafont, S.3    Astier, J.P.4    Boistelle, R.P.5
  • 59
    • 0000333741 scopus 로고    scopus 로고
    • Characterization of single crystals of Photosystem II from the thermophilic cyanobacterium Synechococcus elongatus
    • (Garab, G., Ed.), Kluwer Academic, Dordrecht
    • Zouni, A., Lüneberg, C., Fromme, P., Schubert, W. D., Saenger, W., and Witt, H. T. (1998) Characterization of single crystals of Photosystem II from the thermophilic cyanobacterium Synechococcus elongatus, in Photosynthesis: Mechanisms and Effects (Garab, G., Ed.) Vol. II, pp 925-928, Kluwer Academic, Dordrecht.
    • (1998) Photosynthesis: Mechanisms and Effects , vol.2 , pp. 925-928
    • Zouni, A.1    Lüneberg, C.2    Fromme, P.3    Schubert, W.D.4    Saenger, W.5    Witt, H.T.6
  • 62
    • 0003069455 scopus 로고
    • Crystallization of the PSII-reaction centre
    • (Murata, N., Ed.), Kluwer Academic Press, Dordrecht, The Netherlands
    • Adir, N., Okamura, M. Y., and Feher, G. (1992) Crystallization of the PSII-reaction centre, in Research in Photosynthesis (Murata, N., Ed.) pp 195-198, Kluwer Academic Press, Dordrecht, The Netherlands.
    • (1992) Research in Photosynthesis , pp. 195-198
    • Adir, N.1    Okamura, M.Y.2    Feher, G.3
  • 63
    • 0033119743 scopus 로고    scopus 로고
    • Crystallization of the oxygen-evolving reaction centre of photosystem II in nine different detergent mixtures
    • Adir, N. (1999) Crystallization of the oxygen-evolving reaction centre of photosystem II in nine different detergent mixtures, Acta Crystallogr. D55, 891-894.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 891-894
    • Adir, N.1
  • 64
    • 0030007698 scopus 로고    scopus 로고
    • Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II
    • Nugent, J. H. (1996) Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II, Eur. J. Biochem. 237, 519-531.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 519-531
    • Nugent, J.H.1
  • 65
    • 0031041452 scopus 로고    scopus 로고
    • Characterization of the low molecular weight photosystem II reaction center subunits and their light-induced modifications by mass spectrometry
    • Sharma, J., Panico, M., Barber, J., and Morris, H. R. (1997) Characterization of the low molecular weight photosystem II reaction center subunits and their light-induced modifications by mass spectrometry, J. Biol. Chem. 272, 3935-3943.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3935-3943
    • Sharma, J.1    Panico, M.2    Barber, J.3    Morris, H.R.4
  • 66
    • 0032568955 scopus 로고    scopus 로고
    • Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes
    • Zheleva, D., Sharma, J., Panico, M., Morris, H. R., and Barber, J. (1998) Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes, J. Biol. Chem. 273, 16122-16127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16122-16127
    • Zheleva, D.1    Sharma, J.2    Panico, M.3    Morris, H.R.4    Barber, J.5
  • 67
    • 0031860682 scopus 로고    scopus 로고
    • Multiple crystal types reveal photosystem II to be a dimer
    • Lyon, M. K. (1998) Multiple crystal types reveal photosystem II to be a dimer, Biochim. Biophys. Acta 1364, 403-419.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 403-419
    • Lyon, M.K.1


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