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Volumn 1777, Issue 1, 2008, Pages 94-103

Unfolding of C-phycocyanin followed by loss of non-covalent chromophore-protein interactions. 1. Equilibrium experiments

Author keywords

Biliprotein; Chromophore protein interaction; Optical spectroscopy; Protein dissociation; Protein folding; Protein mobility

Indexed keywords

PHYCOCYANIN; PROTEIN;

EID: 37549052534     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.10.009     Document Type: Article
Times cited : (61)

References (85)
  • 1
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton T.E. (Ed), W.H. Freeman and Co, New York
    • Ptitsyn O.B. The molten globule state. In: Creighton T.E. (Ed). Protein Folding (1992), W.H. Freeman and Co, New York 243-300
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 2
    • 84889861227 scopus 로고    scopus 로고
    • Equilibrium and kinetically observed molten globule states
    • Buchner J., and Kiefhaber T. (Eds), Wiley-VCH, Weinheim
    • Maki K., Kamagata K., and Kuwajima K. Equilibrium and kinetically observed molten globule states. In: Buchner J., and Kiefhaber T. (Eds). Protein Folding Handbook vol. 2 (2005), Wiley-VCH, Weinheim 856-883
    • (2005) Protein Folding Handbook , vol.2 , pp. 856-883
    • Maki, K.1    Kamagata, K.2    Kuwajima, K.3
  • 3
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke R., and Lilie H. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53 (2000) 329-401
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 4
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross roads: which way to go?
    • Uversky V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross roads: which way to go?. Cell. Mol. Life Sci. 60 (2003) 1852-1871
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 5
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., and Hayer-Hart M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hart, M.2
  • 9
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • Ostermann A., Waschipky R., Parak F.G., and Nienhaus G.U. Ligand binding and conformational motions in myoglobin. Nature 404 (2000) 205-208
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F.G.3    Nienhaus, G.U.4
  • 10
    • 0141918782 scopus 로고    scopus 로고
    • Proteins in action: the physics of structural fluctuations and conformational changes
    • Parak F.G. Proteins in action: the physics of structural fluctuations and conformational changes. Curr. Opin. Struct. Biol. 13 (2003) 552-557
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 552-557
    • Parak, F.G.1
  • 12
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science (1991) 1598-1603
    • (1991) Science , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 13
    • 0347949633 scopus 로고    scopus 로고
    • Molecular probes: what is the range of their interaction with the environment?
    • Lesch H., Schlichter J., Friedrich J., and Vanderkooi J.M. Molecular probes: what is the range of their interaction with the environment?. Biophys. J. 86 (2004) 467-472
    • (2004) Biophys. J. , vol.86 , pp. 467-472
    • Lesch, H.1    Schlichter, J.2    Friedrich, J.3    Vanderkooi, J.M.4
  • 14
    • 0023645201 scopus 로고
    • Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1. and 2.5 A resolution - a common principle of phycobilin-protein interaction
    • Schirmer T., Bode W., and Huber R. Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1. and 2.5 A resolution - a common principle of phycobilin-protein interaction. J. Mol. Biol. 196 (1987) 677-695
    • (1987) J. Mol. Biol. , vol.196 , pp. 677-695
    • Schirmer, T.1    Bode, W.2    Huber, R.3
  • 15
    • 0033047094 scopus 로고    scopus 로고
    • Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly
    • Stec B., Troxler R.F., and Teeter M.M. Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly. Biophys. J. 76 (1999) 2912-2921
    • (1999) Biophys. J. , vol.76 , pp. 2912-2921
    • Stec, B.1    Troxler, R.F.2    Teeter, M.M.3
  • 16
    • 0034989667 scopus 로고    scopus 로고
    • Structure of C-phycocyanin from Spirulina Platensis at 2.2 Angstrom resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes
    • Wang X.Q., Li L.N., Chang W.R., Zhang J.P., Gui L.L., Guo B.J., and Liang D.C. Structure of C-phycocyanin from Spirulina Platensis at 2.2 Angstrom resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes. Acta Crystallogr., D Biol. Crystallogr. 57 (2001) 784-792
    • (2001) Acta Crystallogr., D Biol. Crystallogr. , vol.57 , pp. 784-792
    • Wang, X.Q.1    Li, L.N.2    Chang, W.R.3    Zhang, J.P.4    Gui, L.L.5    Guo, B.J.6    Liang, D.C.7
  • 17
    • 0037010843 scopus 로고    scopus 로고
    • Refined structure of C-phycocyanin from the cyanobacterium Synechococcus vulcanus at 1.6 A: insights into the role of solvent molecules in thermal stability and co-factor structure
    • Adir N., Vainer R., and Lerner N. Refined structure of C-phycocyanin from the cyanobacterium Synechococcus vulcanus at 1.6 A: insights into the role of solvent molecules in thermal stability and co-factor structure. Biochim. Biophys. Acta 1556 (2002) 168-174
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 168-174
    • Adir, N.1    Vainer, R.2    Lerner, N.3
  • 18
    • 0003123963 scopus 로고
    • Phycobilisome and phycobiliprotein structures
    • Bryant D.A. (Ed), Kluwer, Dordrecht
    • Sidler W.A. Phycobilisome and phycobiliprotein structures. In: Bryant D.A. (Ed). The Molecular Biology of Cyanobacteria (1994), Kluwer, Dordrecht 139-216
    • (1994) The Molecular Biology of Cyanobacteria , pp. 139-216
    • Sidler, W.A.1
  • 19
    • 37549069369 scopus 로고
    • Circular dichroism of C-phycocyanin: origin of optical activity in denaturated biliproteins and evidence for an intermediate during unfolding
    • Lehner H., and Scheer H. Circular dichroism of C-phycocyanin: origin of optical activity in denaturated biliproteins and evidence for an intermediate during unfolding. Z. Naturforsch. 38c (1983) 353-358
    • (1983) Z. Naturforsch. , vol.38 c , pp. 353-358
    • Lehner, H.1    Scheer, H.2
  • 20
    • 0018569738 scopus 로고
    • The protein chromophore bond in B-phycoerythrin from Porphyridium cruentum
    • Köst-Reyes E., and Köst H.-P. The protein chromophore bond in B-phycoerythrin from Porphyridium cruentum. Eur. J. Biochem. 102 (1979) 83-91
    • (1979) Eur. J. Biochem. , vol.102 , pp. 83-91
    • Köst-Reyes, E.1    Köst, H.-P.2
  • 21
    • 0002427093 scopus 로고
    • Phycobiliproteins: molecular aspects of photosynthetic antenna systems
    • Fong F.K. (Ed), Springer, Berlin
    • Scheer H. Phycobiliproteins: molecular aspects of photosynthetic antenna systems. In: Fong F.K. (Ed). Light Reaction Path of Photosynthesis (1982), Springer, Berlin 7-45
    • (1982) Light Reaction Path of Photosynthesis , pp. 7-45
    • Scheer, H.1
  • 22
    • 33845353161 scopus 로고    scopus 로고
    • The pigments
    • Green B., and Parson W. (Eds), Kluwer, Dordrecht
    • Scheer H. The pigments. In: Green B., and Parson W. (Eds). Light-Harvesting Antennas in Photosynthesis (2003), Kluwer, Dordrecht 29-81
    • (2003) Light-Harvesting Antennas in Photosynthesis , pp. 29-81
    • Scheer, H.1
  • 24
    • 0000370919 scopus 로고
    • Adaptive variations in phycobilisome structure
    • Glazer A.N. Adaptive variations in phycobilisome structure. Adv. Mol. Cell Biol. 10 (1994) 119-149
    • (1994) Adv. Mol. Cell Biol. , vol.10 , pp. 119-149
    • Glazer, A.N.1
  • 25
    • 0029305364 scopus 로고
    • Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 2. Trimers
    • Debreczeny M.P., Sauer K., Zhou J., and Bryant D.A. Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 2. Trimers. J. Phys. Chem. 99 (1995) 8420-8431
    • (1995) J. Phys. Chem. , vol.99 , pp. 8420-8431
    • Debreczeny, M.P.1    Sauer, K.2    Zhou, J.3    Bryant, D.A.4
  • 26
    • 0029307218 scopus 로고
    • Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 1. monomers
    • Debreczeny M.P., Sauer K., Zhou J., and Bryant D.A. Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 1. monomers. J. Phys. Chem. 99 (1995) 8412-8419
    • (1995) J. Phys. Chem. , vol.99 , pp. 8412-8419
    • Debreczeny, M.P.1    Sauer, K.2    Zhou, J.3    Bryant, D.A.4
  • 27
    • 0000906034 scopus 로고
    • Phycocyanin in physical-chemical studies (review)
    • Berns D.S., and Maccoll R. Phycocyanin in physical-chemical studies (review). Chem. Rev. 89 (1989) 807-825
    • (1989) Chem. Rev. , vol.89 , pp. 807-825
    • Berns, D.S.1    Maccoll, R.2
  • 28
    • 0004519819 scopus 로고
    • The microenvironment around the chromophores and its changes due to the association states in C-phycocyanin isolated from the cyanobacterium Mastigocladus-laminosus
    • Mimuro M., Rümbeli R., Fuüistaller P., and Zuber H. The microenvironment around the chromophores and its changes due to the association states in C-phycocyanin isolated from the cyanobacterium Mastigocladus-laminosus. Biochim. Biophys. Acta 851 (1986) 447-456
    • (1986) Biochim. Biophys. Acta , vol.851 , pp. 447-456
    • Mimuro, M.1    Rümbeli, R.2    Fuüistaller, P.3    Zuber, H.4
  • 30
    • 33749363635 scopus 로고    scopus 로고
    • The free energy of dissociation of oligomeric structure in phycocyanin is not linear with denaturant
    • Thoren K.L., Connell K.B., Robinson T.E., Shellhamer D.D., Tammaro M.S., and Gindt Y.M. The free energy of dissociation of oligomeric structure in phycocyanin is not linear with denaturant. Biochemistry 45 (2006) 12050-12059
    • (2006) Biochemistry , vol.45 , pp. 12050-12059
    • Thoren, K.L.1    Connell, K.B.2    Robinson, T.E.3    Shellhamer, D.D.4    Tammaro, M.S.5    Gindt, Y.M.6
  • 31
    • 33845331391 scopus 로고    scopus 로고
    • Three-stage refolding/unfolding of the dual-color β-subunit in R-phycocyanin from Polysiphonia urceolata
    • Ma Y., Xie J., Zhang C., and Zhao J. Three-stage refolding/unfolding of the dual-color β-subunit in R-phycocyanin from Polysiphonia urceolata. Biochem. Biophys. Res. Commun. 352 (2007) 787-793
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 787-793
    • Ma, Y.1    Xie, J.2    Zhang, C.3    Zhao, J.4
  • 32
    • 51249189413 scopus 로고
    • Laboratory culture of thermophilic cyanophytes
    • Castenholz R.W. Laboratory culture of thermophilic cyanophytes. Schweizer. Z. Hydrol. 35 (1970) 538-551
    • (1970) Schweizer. Z. Hydrol. , vol.35 , pp. 538-551
    • Castenholz, R.W.1
  • 34
    • 0004471243 scopus 로고
    • Isolation and biliprotein characterization of phycobilisomes from the thermophilic cyanobacterium Mastigocladus laminosus Cohn
    • Nies M., and Wehrmeyer W. Isolation and biliprotein characterization of phycobilisomes from the thermophilic cyanobacterium Mastigocladus laminosus Cohn. Planta 150 (1980) 330-337
    • (1980) Planta , vol.150 , pp. 330-337
    • Nies, M.1    Wehrmeyer, W.2
  • 35
    • 0036411681 scopus 로고    scopus 로고
    • Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides
    • Wiegand G., Parbel A., Seifert M.H., Holak T.A., and Reuter W. Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides. Eur J Biochem 269 (2002) 5046-5055
    • (2002) Eur J Biochem , vol.269 , pp. 5046-5055
    • Wiegand, G.1    Parbel, A.2    Seifert, M.H.3    Holak, T.A.4    Reuter, W.5
  • 36
    • 84988077134 scopus 로고
    • Fast preparative isoelectric focusing of phycocyanin subunits in layers of granulated gels
    • Köst-Reyes E., Schneider S., John W., Fischer R., Scheer H., and Köst H.-P. Fast preparative isoelectric focusing of phycocyanin subunits in layers of granulated gels. Electrophoresis 8 (1988) 335-336
    • (1988) Electrophoresis , vol.8 , pp. 335-336
    • Köst-Reyes, E.1    Schneider, S.2    John, W.3    Fischer, R.4    Scheer, H.5    Köst, H.-P.6
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Lämmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Lämmli, U.K.1
  • 38
    • 0022486877 scopus 로고
    • Visualization of bilin-linked peptides and proteins in polyacrylamide gels
    • Berkelman T., and Lagarias J.C. Visualization of bilin-linked peptides and proteins in polyacrylamide gels. Anal. Biochem. 156 (1986) 194-201
    • (1986) Anal. Biochem. , vol.156 , pp. 194-201
    • Berkelman, T.1    Lagarias, J.C.2
  • 39
    • 0015935166 scopus 로고
    • Chromophore content of blue-green algal phycobiliproteins
    • Glazer A.N., and Fang S. Chromophore content of blue-green algal phycobiliproteins. J. Biol. Chem. 248 (1973) 659-662
    • (1973) J. Biol. Chem. , vol.248 , pp. 659-662
    • Glazer, A.N.1    Fang, S.2
  • 40
    • 4444269438 scopus 로고    scopus 로고
    • Analysis and reconstitution of phycobiliproteins: methods for the characterization of bilin attachment reactions
    • Smith A.G., and Witty M. (Eds), Humana Press, Totowa, NJ, USA
    • Schluchter W.M., and Bryant D.A. Analysis and reconstitution of phycobiliproteins: methods for the characterization of bilin attachment reactions. In: Smith A.G., and Witty M. (Eds). Heme, Chlorophyll, and Bilins (2002), Humana Press, Totowa, NJ, USA 311-334
    • (2002) Heme, Chlorophyll, and Bilins , pp. 311-334
    • Schluchter, W.M.1    Bryant, D.A.2
  • 41
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from CD
    • Sreerama N., and Woody R.W. A self-consistent method for the analysis of protein secondary structure from CD. Anal. Biochem. 209 (1993) 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 42
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: comparison on CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N.W.R.W. Estimation of protein secondary structure from CD spectra: comparison on CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.W.R.W.1
  • 43
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and is β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., and Woody R.W. Estimation of the number of α-helical and is β-strand segments in proteins using circular dichroism spectroscopy. Prot. Sci. 8 (1999) 370-380
    • (1999) Prot. Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Woody, R.W.2
  • 44
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman J.A. Solvent denaturation. Biopolymers 17 (1978) 1305-1322
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 45
    • 84989738095 scopus 로고
    • Origin of the red-shifted absorption in phycocyanin 632 from Mastigocladus laminosus
    • Gottschalk L., Fischer R., Lottspeich F., and Scheer H. Origin of the red-shifted absorption in phycocyanin 632 from Mastigocladus laminosus. Photochem. Photobiol. 54 (1991) 283-288
    • (1991) Photochem. Photobiol. , vol.54 , pp. 283-288
    • Gottschalk, L.1    Fischer, R.2    Lottspeich, F.3    Scheer, H.4
  • 46
    • 0022555873 scopus 로고
    • Folding intermediates studied by circular dichroism
    • Labhardt A.M. Folding intermediates studied by circular dichroism. Methods Enzymol. 131 (1986) 126-135
    • (1986) Methods Enzymol. , vol.131 , pp. 126-135
    • Labhardt, A.M.1
  • 47
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace N.C. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, N.C.1
  • 48
    • 37549057653 scopus 로고
    • Survey of experimental results obtained by various methods in protein-denaturation studies
    • Lapanje S. (Ed), New York
    • Lapanje S. Survey of experimental results obtained by various methods in protein-denaturation studies. In: Lapanje S. (Ed). Physicochemical Aspects of Protein Denaturation (1978), New York
    • (1978) Physicochemical Aspects of Protein Denaturation
    • Lapanje, S.1
  • 49
    • 0021414377 scopus 로고
    • Spectroscopic properties of tetrapyrroles on denatured biliproteins
    • Guard-Friar D., and Maccoll R. Spectroscopic properties of tetrapyrroles on denatured biliproteins. Arch. Biochem. Biophys. 230 (1984) 300-305
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 300-305
    • Guard-Friar, D.1    Maccoll, R.2
  • 50
    • 9644310200 scopus 로고    scopus 로고
    • Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains
    • Möglich A., Krieger F., and Kiefhaber T. Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains. J. Mol. Biol. 345 (2004) 153-162
    • (2004) J. Mol. Biol. , vol.345 , pp. 153-162
    • Möglich, A.1    Krieger, F.2    Kiefhaber, T.3
  • 51
    • 84989723688 scopus 로고
    • Förster transfer calculations based on crystal structure data from Agmenellum quadruplicatum C-phycocyanin
    • Sauer K., Scheer H., and Sauer P. Förster transfer calculations based on crystal structure data from Agmenellum quadruplicatum C-phycocyanin. Photochem. Photobiol. 46 (1987) 427-440
    • (1987) Photochem. Photobiol. , vol.46 , pp. 427-440
    • Sauer, K.1    Scheer, H.2    Sauer, P.3
  • 52
    • 0000393126 scopus 로고
    • Solution conformations, photophysics, and photochemistry of bili-pigments - bilirubin and biliverdin dimethylesters and related linear tetrapyrroles
    • Braslavsky S.E., Holzwarth A.R., and Schaffner K. Solution conformations, photophysics, and photochemistry of bili-pigments - bilirubin and biliverdin dimethylesters and related linear tetrapyrroles. Angew. Chem., Int. Ed. Engl. 22 (1983) 656-674
    • (1983) Angew. Chem., Int. Ed. Engl. , vol.22 , pp. 656-674
    • Braslavsky, S.E.1    Holzwarth, A.R.2    Schaffner, K.3
  • 54
    • 0030695502 scopus 로고    scopus 로고
    • Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus
    • Parbel A., Zhao K.H., Breton J., and Scheer H. Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus. Photosynth. Res. 54 (1997) 25-34
    • (1997) Photosynth. Res. , vol.54 , pp. 25-34
    • Parbel, A.1    Zhao, K.H.2    Breton, J.3    Scheer, H.4
  • 55
    • 0009548309 scopus 로고
    • UV-visible absorption and circular dichroism spectra of the subunits of C-phycocyanin. II. A quantitative discussion of the chromophore-protein and chromophore-chromophore interactions in the β-subunit
    • Scharnagl C., and Schneider S. UV-visible absorption and circular dichroism spectra of the subunits of C-phycocyanin. II. A quantitative discussion of the chromophore-protein and chromophore-chromophore interactions in the β-subunit. J. Photochem. Photobiol. B. 8 (1991) 129-157
    • (1991) J. Photochem. Photobiol. B. , vol.8 , pp. 129-157
    • Scharnagl, C.1    Schneider, S.2
  • 56
    • 0000165422 scopus 로고
    • Monomeric C-phycocyanin at room temperature and 77 K: resolution of the absorption and fluorescence spectra of the initial chromophores and the energy-transfer rate constants
    • Debreczeny M.P., Sauer K., Zhou J., and Bryant D.A. Monomeric C-phycocyanin at room temperature and 77 K: resolution of the absorption and fluorescence spectra of the initial chromophores and the energy-transfer rate constants. J. Phys. Chem. 97 (1993) 9852-9862
    • (1993) J. Phys. Chem. , vol.97 , pp. 9852-9862
    • Debreczeny, M.P.1    Sauer, K.2    Zhou, J.3    Bryant, D.A.4
  • 57
    • 45449125524 scopus 로고
    • Excitation transfer in C-phycocyanin. Förster transfer rate and exciton calculations based on new crystal structure data for C-phycocyanins from Agmenellum quadruplicatum and Mastigocladus laminosus
    • Sauer K., and Scheer H. Excitation transfer in C-phycocyanin. Förster transfer rate and exciton calculations based on new crystal structure data for C-phycocyanins from Agmenellum quadruplicatum and Mastigocladus laminosus. Biochim. Biophys. Acta 936 (1988) 157-170
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 157-170
    • Sauer, K.1    Scheer, H.2
  • 58
    • 0000511212 scopus 로고
    • Comparison of the stability of phycocyanins from thermophilic, mesophilic, psychrophilic algae
    • Chen C.H., and Berns D.S. Comparison of the stability of phycocyanins from thermophilic, mesophilic, psychrophilic algae. Biophys. Chem. 8 (1978) 191-202
    • (1978) Biophys. Chem. , vol.8 , pp. 191-202
    • Chen, C.H.1    Berns, D.S.2
  • 59
    • 0033524469 scopus 로고    scopus 로고
    • Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant
    • Gokhale R.S., Ray S.S., Balaram H., and Balaram P. Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant. Biochemistry 38 (1999) 423-431
    • (1999) Biochemistry , vol.38 , pp. 423-431
    • Gokhale, R.S.1    Ray, S.S.2    Balaram, H.3    Balaram, P.4
  • 60
    • 0034633885 scopus 로고    scopus 로고
    • Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate
    • Hornby J.A., Luo J.K., Stevens J.M., Wallace L.A., Kaplan W., Armstrong R.N., and Dirr H.W. Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate. Biochemistry 39 (2000) 12336-12344
    • (2000) Biochemistry , vol.39 , pp. 12336-12344
    • Hornby, J.A.1    Luo, J.K.2    Stevens, J.M.3    Wallace, L.A.4    Kaplan, W.5    Armstrong, R.N.6    Dirr, H.W.7
  • 62
    • 0027142791 scopus 로고
    • Reconstitution of allophycocyanin from Mastigocladus laminosus with isolated linker polypeptide
    • Gottschalk L., Lottspeich F., and Scheer H. Reconstitution of allophycocyanin from Mastigocladus laminosus with isolated linker polypeptide. Photochem. Photobiol. 58 (1993) 761-767
    • (1993) Photochem. Photobiol. , vol.58 , pp. 761-767
    • Gottschalk, L.1    Lottspeich, F.2    Scheer, H.3
  • 63
    • 20444437856 scopus 로고    scopus 로고
    • Model for the phycobilisome rod with interlocking disks based on domain-weighted linker-polypeptide sequence homologies of Mastigocladus laminosus
    • Parbel A., and Scheer H. Model for the phycobilisome rod with interlocking disks based on domain-weighted linker-polypeptide sequence homologies of Mastigocladus laminosus. Int. J. Photoenergy 2 (2000) 31-40
    • (2000) Int. J. Photoenergy , vol.2 , pp. 31-40
    • Parbel, A.1    Scheer, H.2
  • 65
    • 0028595909 scopus 로고
    • Femtosecond spectral and anisotropy study of excitation energy transfer between neighbouring alpha-80 and beta 81 chromophores of allophycocyanin trimers
    • Sharkov A.V., Kryukov I.V., Khoroshilov E.V., Kryukov P.G., Fischer R., Scheer H., and Gillbro T. Femtosecond spectral and anisotropy study of excitation energy transfer between neighbouring alpha-80 and beta 81 chromophores of allophycocyanin trimers. Biochim. Biophys. Acta 1188 (1994) 349-356
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 349-356
    • Sharkov, A.V.1    Kryukov, I.V.2    Khoroshilov, E.V.3    Kryukov, P.G.4    Fischer, R.5    Scheer, H.6    Gillbro, T.7
  • 67
    • 0002531047 scopus 로고
    • Studies on chromophore coupling in isolated phycobiliproteins. 4. Femtosecond transient absorption study of ultrafast excited state dynamics in trimeric phycoerythrocyanin complexes
    • Hucke M., Schweitzer G., Holzwarth A.R., Sidler W., and Zuber H. Studies on chromophore coupling in isolated phycobiliproteins. 4. Femtosecond transient absorption study of ultrafast excited state dynamics in trimeric phycoerythrocyanin complexes. Photochem. Photobiol. 57 (1993) 76-80
    • (1993) Photochem. Photobiol. , vol.57 , pp. 76-80
    • Hucke, M.1    Schweitzer, G.2    Holzwarth, A.R.3    Sidler, W.4    Zuber, H.5
  • 68
    • 0000330064 scopus 로고
    • Phycobilisomes
    • Gantt E. Phycobilisomes. Ann. Rev. Physiol. 32 (1981) 327-347
    • (1981) Ann. Rev. Physiol. , vol.32 , pp. 327-347
    • Gantt, E.1
  • 70
    • 0027466720 scopus 로고
    • Molecular assembly of the phycobilisomes from the cyanobacterium Mastigocladus laminosus
    • Reuter W., and Nickel-Reuter C. Molecular assembly of the phycobilisomes from the cyanobacterium Mastigocladus laminosus. J. Photochem. Photobiol., B 18 (1993) 51-66
    • (1993) J. Photochem. Photobiol., B , vol.18 , pp. 51-66
    • Reuter, W.1    Nickel-Reuter, C.2
  • 71
    • 84989688257 scopus 로고
    • Isolation, characterization and reconstitution of phycobiliprotein rod-core linker polypeptide complexes from the phycobilisome of Mastigocladus-laminosus
    • Glauser M., Sidler W., and Zuber H. Isolation, characterization and reconstitution of phycobiliprotein rod-core linker polypeptide complexes from the phycobilisome of Mastigocladus-laminosus. Photochem. Photobiol. 57 (1993) 344-351
    • (1993) Photochem. Photobiol. , vol.57 , pp. 344-351
    • Glauser, M.1    Sidler, W.2    Zuber, H.3
  • 72
    • 0015935094 scopus 로고
    • Formation of hybrid proteins from the alpha- and beta-subunits of phycocyanins from unicellular and filamentous blue-green algae
    • Glazer A.N., and Fang S. Formation of hybrid proteins from the alpha- and beta-subunits of phycocyanins from unicellular and filamentous blue-green algae. J. Biol. Chem. 248 (1973) 663-671
    • (1973) J. Biol. Chem. , vol.248 , pp. 663-671
    • Glazer, A.N.1    Fang, S.2
  • 73
    • 0020770057 scopus 로고
    • The complete amino-acid-sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus
    • Füglistaller P., Suter F., and Zuber H. The complete amino-acid-sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus. Hoppe Seyler's Z. Physiol. Chem. 364 (1983) 691-712
    • (1983) Hoppe Seyler's Z. Physiol. Chem. , vol.364 , pp. 691-712
    • Füglistaller, P.1    Suter, F.2    Zuber, H.3
  • 74
    • 84981661816 scopus 로고
    • Synthesis and reactivity of 22,23-methylene,-2,3,17,18-tetramethyl-23-hydro-1,19-(21H,24H)-bilindion-10-enium trifluoroacetate
    • De Groot J.A., Vandersteen R., and Lugtenburg J. Synthesis and reactivity of 22,23-methylene,-2,3,17,18-tetramethyl-23-hydro-1,19-(21H,24H)-bilindion-10-enium trifluoroacetate. Rec. Trav. Chim. 101 (1982) 263-266
    • (1982) Rec. Trav. Chim. , vol.101 , pp. 263-266
    • De Groot, J.A.1    Vandersteen, R.2    Lugtenburg, J.3
  • 75
    • 37549064378 scopus 로고    scopus 로고
    • J. Gottstein, Der Einfluβ Von Grenzflächenaktiven Substanzen Auf Die Selbstaggregation Von Chlorophyllen Und Phycocyaninen., Dissertation, Universität München. (1990).
  • 76
    • 0344988758 scopus 로고
    • Picosecond time-resolved fluorescence of phycobiliproteins: subunits of phycocyanin from Mastigocladus laminosus
    • Fischer R., Gottstein J., Scheer H., Geiselhart P., and Schneider S. Picosecond time-resolved fluorescence of phycobiliproteins: subunits of phycocyanin from Mastigocladus laminosus. J. Photochem. Photobiol., B 5 (1990) 151-165
    • (1990) J. Photochem. Photobiol., B , vol.5 , pp. 151-165
    • Fischer, R.1    Gottstein, J.2    Scheer, H.3    Geiselhart, P.4    Schneider, S.5
  • 77
    • 37549040604 scopus 로고    scopus 로고
    • S. Böhm, α-Phycoerythrocyanin: Dynamik Des Reversiblen Photochromismus Und Lyase-Katalysierte Holoproteinassemblierung, Dissertation, Ludwig-Maximilians-Universität, München (2006).
  • 78
    • 84985063331 scopus 로고
    • Isophorcarubin - a conformationally restricted and highly fluorescent bilirubin
    • Kufer W., Scheer H., and Holzwarth A.R. Isophorcarubin - a conformationally restricted and highly fluorescent bilirubin. Isr. J. Chem. 23 (1983) 233-240
    • (1983) Isr. J. Chem. , vol.23 , pp. 233-240
    • Kufer, W.1    Scheer, H.2    Holzwarth, A.R.3
  • 79
    • 84987055068 scopus 로고
    • Synthesis and spectroscopic study of 1,1′-methylene-2,2′-pyrromethen-5(1H)-one and its 3,4-dihydro and 2,3,4,6-tetrahydro derivate
    • Van Es J.J.G.S., Koek J.H., Erkelens C., and Lugtenburg J. Synthesis and spectroscopic study of 1,1′-methylene-2,2′-pyrromethen-5(1H)-one and its 3,4-dihydro and 2,3,4,6-tetrahydro derivate. Rec. Trav. Chim. 105 (1986) 360-367
    • (1986) Rec. Trav. Chim. , vol.105 , pp. 360-367
    • Van Es, J.J.G.S.1    Koek, J.H.2    Erkelens, C.3    Lugtenburg, J.4
  • 80
    • 0020184637 scopus 로고
    • Theoretical studies of biliprotein chromophores and related bile pigments by molecular orbital and Ramachandran type calculation
    • Scheer H., Formanek H., and Schneider S. Theoretical studies of biliprotein chromophores and related bile pigments by molecular orbital and Ramachandran type calculation. Photochem. Photobiol. 36 (1982) 259-272
    • (1982) Photochem. Photobiol. , vol.36 , pp. 259-272
    • Scheer, H.1    Formanek, H.2    Schneider, S.3
  • 81
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 82
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin M., and Baldwin R.L. Two forms of the pH 4 folding intermediate of apomyoglobin. J. Mol. Biol. 276 (1998) 491-504
    • (1998) J. Mol. Biol. , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.L.2
  • 83
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y., Takahashi N., and Fink A.L. Mechanism of acid-induced folding of proteins. Biochemistry 29 (1990) 3480-3488
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 84
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh S.N., Kay M.S., and Baldwin R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 5446-5450
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3


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