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Volumn 15, Issue 8, 2006, Pages 1977-1986

The oligomeric state and stability of the mannitol transporter, EnzymeIImtl, from Escherichia coli: A fluorescence correlation spectroscopy study

Author keywords

EnzymeII; Fluorescence correlation spectroscopy; Mannitol transporter; Oligomeric stability; Oligomeric state

Indexed keywords

BUFFER; CARRIER PROTEIN; CYSTEINE; MANNITOL TRANSPORTER; MUTANT PROTEIN; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33746473476     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062113906     Document Type: Article
Times cited : (5)

References (56)
  • 1
    • 0025332692 scopus 로고
    • UhpT, the sugar phosphate antiporter of Escherichia coli, functions as a monomer
    • Ambudkar, S.V., Anantharam, V., and Maloney, P.C. 1990. UhpT, the sugar phosphate antiporter of Escherichia coli , functions as a monomer. J. Biol. Chem. 265: 12287-12292.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12287-12292
    • Ambudkar, S.V.1    Anantharam, V.2    Maloney, P.C.3
  • 2
    • 36749107042 scopus 로고
    • Fluorescence correlation spectroscopy as a probe of molecular dynamics
    • Aragón, S.R. and Pecora, R. 1976. Fluorescence correlation spectroscopy as a probe of molecular dynamics. J. Chem. Phys. 64: 1791-1803.
    • (1976) J. Chem. Phys. , vol.64 , pp. 1791-1803
    • Aragón, S.R.1    Pecora, R.2
  • 3
    • 0028361812 scopus 로고
    • Expression, purification and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli
    • Boer, H., Ten Hoeve-Duurkens, R.H., Schuurman-Wolters, G.K., Dijkstra, A., and Robillard, G.T. 1994. Expression, purification and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate- dependent mannitol phosphotransferase system of Escherichia coli. J. Biol. Chem. 269: 17863-17871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17863-17871
    • Boer, H.1    Ten Hoeve-Duurkens, R.H.2    Schuurman-Wolters, G.K.3    Dijkstra, A.4    Robillard, G.T.5
  • 4
    • 0029846910 scopus 로고    scopus 로고
    • Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: Interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants
    • Boer, H., Ten Hoeve-Duurkens, R.H., and Robillard, G.T. 1996. Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: Interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants. Biochemistry 35: 12901-12908.
    • (1996) Biochemistry , vol.35 , pp. 12901-12908
    • Boer, H.1    Ten Hoeve-Duurkens, R.H.2    Robillard, G.T.3
  • 5
    • 0026585760 scopus 로고
    • Structure/function relationships in the Escherichia coli mannitol permease: Identification of regions important for membrane insertion, substrate binding and oligomerization
    • Briggs, C.E., Khandekar, S.S., and Jacobson, G.R. 1992. Structure/function relationships in the Escherichia coli mannitol permease: Identification of regions important for membrane insertion, substrate binding and oligomerization. Res. Microbiol. 143: 139-149.
    • (1992) Res. Microbiol. , vol.143 , pp. 139-149
    • Briggs, C.E.1    Khandekar, S.S.2    Jacobson, G.R.3
  • 7
    • 0033520096 scopus 로고    scopus 로고
    • Membrane protein-ligand interactions in Escherichia coli vesicles and living cells monitored via a biosynthetically incorporated tryptophan analogue
    • Broos, J., Ter Veld, F., and Robillard, G.T. 1999. Membrane protein-ligand interactions in Escherichia coli vesicles and living cells monitored via a biosynthetically incorporated tryptophan analogue. Biochemistry 38: 9798-9803.
    • (1999) Biochemistry , vol.38 , pp. 9798-9803
    • Broos, J.1    Ter Veld, F.2    Robillard, G.T.3
  • 8
    • 0034609525 scopus 로고    scopus 로고
    • Sensitive monitoring of the dynamics of a membrane-bound transport protein by tryptophan phosphorescence spectroscopy
    • Broos, J., Strambini, G.B., Gonnelli, M., Vos, E.P.P., Koolhof, M., and Robillard, G.T. 2000. Sensitive monitoring of the dynamics of a membrane-bound transport protein by tryptophan phosphorescence spectroscopy. Biochemistry 39: 10877-10883.
    • (2000) Biochemistry , vol.39 , pp. 10877-10883
    • Broos, J.1    Strambini, G.B.2    Gonnelli, M.3    Vos, E.P.P.4    Koolhof, M.5    Robillard, G.T.6
  • 9
    • 0037134857 scopus 로고    scopus 로고
    • The smallest resonance energy transfer acceptor for tryptophan
    • Broos, J., Pas, H.H., and Robillard, G.T. 2002. The smallest resonance energy transfer acceptor for tryptophan. J. Am. Chem. Soc. 124: 6812-6813.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6812-6813
    • Broos, J.1    Pas, H.H.2    Robillard, G.T.3
  • 10
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
    • Casey, J.R. and Reithmeier, R.A.F. 1991. Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266: 15726-15737.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 11
    • 0028229903 scopus 로고
    • Sorting single molecules. Applications to diagnostics and evolutionary biotechnology
    • Eigen, M. and Rigler, R. 1994. Sorting single molecules. Applications to diagnostics and evolutionary biotechnology. Proc. Natl. Acad. Sci. 91: 5740-5747.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 12
    • 0034721921 scopus 로고    scopus 로고
    • Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergentsolubilized and membrane-reconstituted state
    • Friesen, R.H., Knol, J., and Poolman, B. 2000. Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergentsolubilized and membrane-reconstituted state. J. Biol. Chem. 275: 33527-33535.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33527-33535
    • Friesen, R.H.1    Knol, J.2    Poolman, B.3
  • 13
    • 20444403768 scopus 로고    scopus 로고
    • Functional interactions between subunits of the lactose transporter from Streptococcus thermophilus
    • Geertsma, E.R., Duurkens, R.H., and Poolman, B. 2005. Functional interactions between subunits of the lactose transporter from Streptococcus thermophilus. J. Mol. Biol. 350: 102-111.
    • (2005) J. Mol. Biol. , vol.350 , pp. 102-111
    • Geertsma, E.R.1    Duurkens, R.H.2    Poolman, B.3
  • 14
    • 0035916942 scopus 로고    scopus 로고
    • +-antiporter of Escherichia coli in the membrane and its functional and structural consequences
    • +-antiporter of Escherichia coli in the membrane and its functional and structural consequences. Biochemistry 40: 3403-3412.
    • (2001) Biochemistry , vol.40 , pp. 3403-3412
    • Gerchman, Y.1    Rimon, A.2    Venturi, M.3    Padan, E.4
  • 15
    • 7044237136 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of molecular motions and kinetics
    • Gösch, M. and Rigler, R. 2005. Fluorescence correlation spectroscopy of molecular motions and kinetics. Adv. Drug Deliv. Rev. 57: 169-190.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 169-190
    • Gösch, M.1    Rigler, R.2
  • 16
    • 0024670303 scopus 로고
    • Deletion mutants of the Escherichia coli K-12 mannitol permease: Dissection of transport-phosphorylation, phospho-exchange, and mannitol-binding activities
    • Grisafi, P.L., Scholle, A., Sugiyama, J., Briggs, C., Jacobson, G.R., and Lengeler, J.W. 1989. Deletion mutants of the Escherichia coli K-12 mannitol permease: Dissection of transport-phosphorylation, phospho-exchange, and mannitol-binding activities. J. Bacteriol. 171: 2719-2727.
    • (1989) J. Bacteriol. , vol.171 , pp. 2719-2727
    • Grisafi, P.L.1    Scholle, A.2    Sugiyama, J.3    Briggs, C.4    Jacobson, G.R.5    Lengeler, J.W.6
  • 17
    • 0037331059 scopus 로고    scopus 로고
    • Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy
    • Haustein, E. and Schwille, P. 2003. Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy. Methods 29: 153-166.
    • (2003) Methods , vol.29 , pp. 153-166
    • Haustein, E.1    Schwille, P.2
  • 18
    • 4744364544 scopus 로고    scopus 로고
    • Single-molecule spectroscopic methods
    • _. 2004. Single-molecule spectroscopic methods. Curr. Opin. Struct. Biol. 14: 531-540.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 531-540
  • 19
    • 0027082962 scopus 로고
    • Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1
    • Hebert, D.N. and Carruthers, A. 1992. Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1. J. Biol. Chem. 267: 23829-23838.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23829-23838
    • Hebert, D.N.1    Carruthers, A.2
  • 21
    • 0024518066 scopus 로고
    • Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions
    • Khandekar, S.S. and Jacobson, G.R. 1989. Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions. J. Cell. Biochem. 39: 207-216.
    • (1989) J. Cell. Biochem. , vol.39 , pp. 207-216
    • Khandekar, S.S.1    Jacobson, G.R.2
  • 22
    • 0021030763 scopus 로고
    • Mannitol-specific enzyme II of the bacterial phosphotransferase system. II. Reconstitution of vectorial transphosphorylation in phospholipid vesicles
    • Leonard, J.E. and Saier Jr., M.H. 1983. Mannitol-specific enzyme II of the bacterial phosphotransferase system. II. Reconstitution of vectorial transphosphorylation in phospholipid vesicles. J. Biol. Chem. 258: 10757-10760.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10757-10760
    • Leonard, J.E.1    Saier Jr., M.H.2
  • 23
    • 0024998164 scopus 로고
    • Subunit structure and activity of the mannitol-specific Enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system solubilized in detergent
    • Lolkema, J.S. and Robillard, G.T. 1990. Subunit structure and activity of the mannitol-specific Enzyme II of the Escherichia coli phosphoenolpyruvate- dependent phosphotransferase system solubilized in detergent. Biochemistry 29: 10120-10125.
    • (1990) Biochemistry , vol.29 , pp. 10120-10125
    • Lolkema, J.S.1    Robillard, G.T.2
  • 25
    • 0027172682 scopus 로고
    • mtl of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli
    • mtl of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Biochemistry 32: 5848-5854.
    • (1993) Biochemistry , vol.32 , pp. 5848-5854
    • Lolkema, J.S.1    Wartna, E.S.2    Robillard, G.T.3
  • 27
    • 0033021689 scopus 로고    scopus 로고
    • Resolution of fluorescence correlation measurements
    • Meseth, U., Wohland, T., Rigler, R., and Vogel, H. 1999. Resolution of fluorescence correlation measurements. Biophys. J. 76: 1619-1631.
    • (1999) Biophys. J. , vol.76 , pp. 1619-1631
    • Meseth, U.1    Wohland, T.2    Rigler, R.3    Vogel, H.4
  • 28
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4: 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 29
    • 0023661104 scopus 로고
    • Bacterial phosph oenolpyruvate-dependent phosphotransferase system: Association state of membrane-bound mannitol-specific enzyme II demonstrated by inactivation
    • Pas, H.H., Ellory, J.C., and Robillard, G.T. 1987. Bacterial phosph oenolpyruvate-dependent phosphotransferase system: Association state of membrane-bound mannitol-specific enzyme II demonstrated by inactivation. Biochemistry 26: 6689-6696.
    • (1987) Biochemistry , vol.26 , pp. 6689-6696
    • Pas, H.H.1    Ellory, J.C.2    Robillard, G.T.3
  • 30
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • Rigler, R., Mets, Ü., Widengren, J., and Kask, P. 1993. Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion. Eur. Biophys. J. 22: 169-175.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, Ü.2    Widengren, J.3    Kask, P.4
  • 31
    • 0023648301 scopus 로고
    • Enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: Protein-protein and protein-phospholipid interactions
    • Robillard, G.T. and Blaauw, M. 1987. Enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: Protein-protein and protein-phospholipid interactions. Biochemistry 26: 5796-5803.
    • (1987) Biochemistry , vol.26 , pp. 5796-5803
    • Robillard, G.T.1    Blaauw, M.2
  • 32
    • 0033045836 scopus 로고    scopus 로고
    • Structure/function studies on the bacterial carbohydrate transporters, enzyme II, of the phosphoenolpyruvate-dependent phosphotransferase system
    • Robillard, G.T. and Broos, J. 1999. Structure/function studies on the bacterial carbohydrate transporters, enzyme II, of the phosphoenolpyruvate- dependent phosphotransferase system. Biochim. Biophys. Acta 1422: 73-104.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 73-104
    • Robillard, G.T.1    Broos, J.2
  • 33
    • 0021767831 scopus 로고
    • Mannitol-specific carrier protein from the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system can be extracted as a dimer from the membrane
    • Roossien, F.F. and Robillard, G.T. 1984. Mannitol-specific carrier protein from the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system can be extracted as a dimer from the membrane. Biochemistry 23: 41-44.
    • (1984) Biochemistry , vol.23 , pp. 41-44
    • Roossien, F.F.1    Robillard, G.T.2
  • 34
    • 0021759012 scopus 로고
    • Kinetics and subunit interaction of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system
    • Roossien, F.F., Blaauw, M., and Robillard, G.T. 1984. Kinetics and subunit interaction of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Biochemistry 23: 4934-4939.
    • (1984) Biochemistry , vol.23 , pp. 4934-4939
    • Roossien, F.F.1    Blaauw, M.2    Robillard, G.T.3
  • 35
    • 0022559180 scopus 로고
    • mtl of the E. coli phosphoenolpyruvate- dependent phosphotransferase system. Cross-linking studies with bifunctional sulfhydryl reagents
    • mtl of the E. coli phosphoenolpyruvate-dependent phosphotransferase system. Cross-linking studies with bifunctional sulfhydryl reagents. FEBS Lett. 196: 284-290.
    • (1986) FEBS Lett. , vol.196 , pp. 284-290
    • Roossien, F.F.1    Van Es-Spiekman, W.2    Robillard, G.T.3
  • 36
    • 0028291250 scopus 로고
    • Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli
    • Sahin-Toth, M., Lawrence, M.C., and Kaback, H.R. 1994. Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli. Proc. Natl. Acad. Sci. 91: 5421-5425.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5421-5425
    • Sahin-Toth, M.1    Lawrence, M.C.2    Kaback, H.R.3
  • 37
    • 0019257775 scopus 로고
    • Catalytic activities associated with the enzymes II of the bacterial phosphotransferase system
    • Saier Jr., M.H. 1980. Catalytic activities associated with the enzymes II of the bacterial phosphotransferase system. J. Supramol. Struct. 14: 281-294.
    • (1980) J. Supramol. Struct. , vol.14 , pp. 281-294
    • Saier Jr., M.H.1
  • 38
    • 0031046661 scopus 로고    scopus 로고
    • A conserved glutamate residue, Glu-257, is important for substrate binding and transport by the Escherichia coli mannitol permease
    • Saraceni-Richards, C.A. and Jacobson, G.R. 1997. A conserved glutamate residue, Glu-257, is important for substrate binding and transport by the Escherichia coli mannitol permease. J. Bacteriol. 179: 1135-1142.
    • (1997) J. Bacteriol. , vol.179 , pp. 1135-1142
    • Saraceni-Richards, C.A.1    Jacobson, G.R.2
  • 39
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille, P., Almes-Meyer, F.J., and Rigler, R. 1997. Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys. J. 72: 1878-1886.
    • (1997) Biophys. J. , vol.72 , pp. 1878-1886
    • Schwille, P.1    Almes-Meyer, F.J.2    Rigler, R.3
  • 40
    • 0022481980 scopus 로고
    • Subunit interactions of the Escherichia coli mannitol permease: Correlation with enzyme activities
    • Stephan, M.M. and Jacobson, G.R. 1986. Subunit interactions of the Escherichia coli mannitol permease: Correlation with enzyme activities. Biochemistry 25: 4046-4051.
    • (1986) Biochemistry , vol.25 , pp. 4046-4051
    • Stephan, M.M.1    Jacobson, G.R.2
  • 41
    • 0024974061 scopus 로고
    • Hydrophilic C-terminal domain of the Escherichia coli mannitol permease: Phosphorylation, functional independence, and evidence for intersubunit phosphotransfer
    • Stephan, M.M., Khandekar, S.S., and Jacobson, G.R. 1989. Hydrophilic C-terminal domain of the Escherichia coli mannitol permease: Phosphorylation, functional independence, and evidence for intersubunit phosphotransfer. Biochemistry 28: 7941-7946.
    • (1989) Biochemistry , vol.28 , pp. 7941-7946
    • Stephan, M.M.1    Khandekar, S.S.2    Jacobson, G.R.3
  • 42
    • 0030586826 scopus 로고    scopus 로고
    • Membrane proteins and impure detergents: Procedures to purify membrane proteins to a degree suitable for tryptophan fluorescence spectroscopy
    • Swaving-Dijkstra, D., Broos, J., and Robillard, G.T. 1996. Membrane proteins and impure detergents: Procedures to purify membrane proteins to a degree suitable for tryptophan fluorescence spectroscopy. Anal. Biochem. 240: 142-147.
    • (1996) Anal. Biochem. , vol.240 , pp. 142-147
    • Swaving-Dijkstra, D.1    Broos, J.2    Robillard, G.T.3
  • 43
    • 1942532338 scopus 로고    scopus 로고
    • New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: An unusual asymmetric homo-dimer
    • Ubarretxena-Belandia, I. and Tate, C.G. 2004. New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: An unusual asymmetric homo-dimer. FEBS Lett. 564: 234-238.
    • (2004) FEBS Lett. , vol.564 , pp. 234-238
    • Ubarretxena-Belandia, I.1    Tate, C.G.2
  • 44
    • 0035918216 scopus 로고    scopus 로고
    • Cysteine cross-linking defines part of the dimer and B/C domain interface of the Escherichia coli mannitol permease
    • Van Montfort, B.A., Schuurman-Wolters, G.K., Duurkens, R.H., Mensen, R., Poolman, B., and Robillard, G.T. 2001. Cysteine cross-linking defines part of the dimer and B/C domain interface of the Escherichia coli mannitol permease. J. Biol. Chem. 276: 12756-12763.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12756-12763
    • Van Montfort, B.A.1    Schuurman-Wolters, G.K.2    Duurkens, R.H.3    Mensen, R.4    Poolman, B.5    Robillard, G.T.6
  • 47
    • 0025845009 scopus 로고
    • Details of mannitol transport in Escherichia coli elucidated by site-specific mutagenesis and complementation of phosphorylation site mutants of the phosphoenolpyruvate-dependent mannitol-specific phosphotransferase system
    • Van Weeghel, R.P., Van der Hoek, Y.Y., Pas, H.H., Elferink, M., Keck, W., and Robillard, G.T. 1991b. Details of mannitol transport in Escherichia coli elucidated by site-specific mutagenesis and complementation of phosphorylation site mutants of the phosphoenolpyruvate-dependent mannitol-specific phosphotransferase system. Biochemistry 30: 1768-1773.
    • (1991) Biochemistry , vol.30 , pp. 1768-1773
    • Van Weeghel, R.P.1    Van Der Hoek, Y.Y.2    Pas, H.H.3    Elferink, M.4    Keck, W.5    Robillard, G.T.6
  • 48
    • 0035875919 scopus 로고    scopus 로고
    • The lactose transport protein is a cooperative dimer with two sugar translocation pathways
    • Veenhoff, L.M., Heuberger, E.H.M.L., and Poolman, B. 2001. The lactose transport protein is a cooperative dimer with two sugar translocation pathways. EMBO J. 20: 3056-3062.
    • (2001) EMBO J. , vol.20 , pp. 3056-3062
    • Veenhoff, L.M.1    Heuberger, E.H.M.L.2    Poolman, B.3
  • 49
    • 1942519794 scopus 로고    scopus 로고
    • Evaluation of the flow-dialysis technique for analysis of protein-ligand interactions: An experimental and a Monte Carlo study
    • Veldhuis, G., Vos, E.P.P., Broos, J., Poolman, B., and Scheek, R.M. 2004. Evaluation of the flow-dialysis technique for analysis of protein-ligand interactions: An experimental and a Monte Carlo study. Biophys. J. 86: 1959-1968.
    • (2004) Biophys. J. , vol.86 , pp. 1959-1968
    • Veldhuis, G.1    Vos, E.P.P.2    Broos, J.3    Poolman, B.4    Scheek, R.M.5
  • 52
    • 0027452390 scopus 로고
    • Role of a conserved histidine residue, His-195, in the activities of the Escherichia coli mannitol permease
    • Weng, Q.-P. and Jacobson, G.R. 1993. Role of a conserved histidine residue, His-195, in the activities of the Escherichia coli mannitol permease. Biochemistry 32: 11211-11216.
    • (1993) Biochemistry , vol.32 , pp. 11211-11216
    • Weng, Q.-P.1    Jacobson, G.R.2
  • 53
    • 0026660314 scopus 로고
    • Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions
    • Weng, Q.-P., Elder, J., and Jacobson, G.R. 1992. Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions. J. Biol. Chem. 267: 19529-19535.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19529-19535
    • Weng, Q.-P.1    Elder, J.2    Jacobson, G.R.3
  • 54
    • 0025259425 scopus 로고
    • Molecular cloning of the C-terminal domain of Escherichia coli D-mannitol permease: Expression, phosphorylation, and complementation with C-terminal permease deletion mutants
    • White, D.W. and Jacobson, G.R. 1990. Molecular cloning of the C-terminal domain of Escherichia coli D-mannitol permease: Expression, phosphorylation, and complementation with C-terminal permease deletion mutants. J. Bacteriol. 172: 1509-1515.
    • (1990) J. Bacteriol. , vol.172 , pp. 1509-1515
    • White, D.W.1    Jacobson, G.R.2
  • 56
    • 85143331539 scopus 로고
    • Detergent phenomena in membrane protein crystallization
    • ed. H. Michel, CRC Press, Boca Raton, FL
    • Zulauf, M. 1991. Detergent phenomena in membrane protein crystallization. In Crystallization of membrane proteins (ed. H. Michel), pp. 53-72, CRC Press, Boca Raton, FL.
    • (1991) Crystallization of Membrane Proteins , pp. 53-72
    • Zulauf, M.1


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