메뉴 건너뛰기




Volumn 47, Issue 11, 2008, Pages 3513-3524

Stability of the glycerol facilitator in detergent solutions

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR EXPLANATION; OLIGOMERIC STATE; SODIUM DODECYL SULFATE (SDS);

EID: 40849106466     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7021409     Document Type: Article
Times cited : (30)

References (84)
  • 1
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer, R., and Tate, C. G. (1995) Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 28, 315-422.
    • (1995) Q. Rev. Biophys , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 2
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11, 397-402.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 3
    • 0037450542 scopus 로고    scopus 로고
    • Assembly and overexpression of membrane proteins in Escherichia coli
    • Drew, D., Froderberg, L., Baars, L., and de Gier, J. W. (2003) Assembly and overexpression of membrane proteins in Escherichia coli. Biochim. Biophys. Acta 1610, 3-10.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 3-10
    • Drew, D.1    Froderberg, L.2    Baars, L.3    de Gier, J.W.4
  • 4
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    von Heijne, G.6
  • 5
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 7
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • Tsai, J., Taylor, R., Chothia, C., and Gerstein, M. (1999) The packing density in proteins: Standard radii and volumes. J. Mol. Biol. 290, 253-266.
    • (1999) J. Mol. Biol , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 8
    • 0023410587 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: Membrane-protein interactions
    • Yeates, T. O., Komiya, H., Rees, D. C., Allen, J. P., and Feher, G. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: Membrane-protein interactions. Proc. Natl. Acad. Sci. U.S.A. 84, 6438-6442.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 6438-6442
    • Yeates, T.O.1    Komiya, H.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 9
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti, C. A., and Remeta, D. P. (2006) Energetics of membrane protein folding and stability. Arch. Biochem. Biophys. 453, 32-53.
    • (2006) Arch. Biochem. Biophys , vol.453 , pp. 32-53
    • Minetti, C.A.1    Remeta, D.P.2
  • 10
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of α-helical integral membrane proteins
    • Mackenzie, K. R. (2006) Folding and stability of α-helical integral membrane proteins. Chem. Rev. 106, 1931-1977.
    • (2006) Chem. Rev , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 11
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • Hong, H., and Tamm, L. K. (2004) Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl. Acad. Sci. U.S.A. 101, 4065-4070.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 12
    • 33845428343 scopus 로고    scopus 로고
    • An unfolding story of helical transmembrane proteins
    • Renthal, R. (2006) An unfolding story of helical transmembrane proteins. Biochemistry 45, 14559-14566.
    • (2006) Biochemistry , vol.45 , pp. 14559-14566
    • Renthal, R.1
  • 13
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H., and Engelman, D. M. (1997) A transmembrane helix dimer: Structure and implications. Science 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 14
    • 8844261812 scopus 로고    scopus 로고
    • Sec-translocase mediated membrane protein biogenesis
    • Dalbey, R. E., and Chen, M. (2004) Sec-translocase mediated membrane protein biogenesis. Biochim. Biophys. Acta 1694, 37-53.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 37-53
    • Dalbey, R.E.1    Chen, M.2
  • 18
    • 0036566310 scopus 로고    scopus 로고
    • A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
    • Bogdanov, M., Heacock, P. N., and Dowhan, W. (2002) A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition. EMBO J. 21, 2107-2116.
    • (2002) EMBO J , vol.21 , pp. 2107-2116
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 19
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function: The hydrophobic matching hypothesis revisited
    • Jensen, M. O., and Mouritsen, O. G. (2004) Lipids do influence protein function: The hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta 1666, 205-226.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 20
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L., and Engelman, D. M. (1990) Membrane protein folding and oligomerization: The two-stage model. Biochemistry 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 21
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and Engelman, D. M. (2000) Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69, 881-922.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 23
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H., and Wimley, W. C. (1999) Membrane protein folding and stability: Physical principles. Annu. Rev. Biophys. Biomol. Struct. 28, 319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 24
    • 0242573122 scopus 로고    scopus 로고
    • Aquaporin water channels: Molecular mechanisms for human diseases
    • Agre, P., and Kozono, D. (2003) Aquaporin water channels: Molecular mechanisms for human diseases. FEBS Lett. 555, 72-78.
    • (2003) FEBS Lett , vol.555 , pp. 72-78
    • Agre, P.1    Kozono, D.2
  • 25
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia, M., Nielsen, S., Engel, A., and Agre, P. (1999) Cellular and molecular biology of the aquaporin water channels. Annu. Rev. Biochem. 68, 425-458.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 28
    • 0019195926 scopus 로고
    • Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli
    • Heller, K. B., Lin, E. C., and Wilson, T. H. (1980) Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. J. Bacteriol. 144, 274-278.
    • (1980) J. Bacteriol , vol.144 , pp. 274-278
    • Heller, K.B.1    Lin, E.C.2    Wilson, T.H.3
  • 30
    • 0028787084 scopus 로고
    • Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli
    • Calamita, G., Bishai, W. R., Preston, G. M., Guggino, W. B., and Agre, P. (1995) Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J. Biol. Chem. 270, 29063-29066.
    • (1995) J. Biol. Chem , vol.270 , pp. 29063-29066
    • Calamita, G.1    Bishai, W.R.2    Preston, G.M.3    Guggino, W.B.4    Agre, P.5
  • 31
    • 85177152424 scopus 로고    scopus 로고
    • Maurel, C., Reizer, J., Schroeder, J. I., Chrispeels, M. J., and Saier, M. H., Jr. (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269, 11869-11872.
    • Maurel, C., Reizer, J., Schroeder, J. I., Chrispeels, M. J., and Saier, M. H., Jr. (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269, 11869-11872.
  • 32
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • Sanders, O. I., Rensing, C., Kuroda, M., Mitra, B., and Rosen, B. P. (1997) Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli. J. Bacteriol. 179, 3365-3367.
    • (1997) J. Bacteriol , vol.179 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 33
    • 0035853028 scopus 로고    scopus 로고
    • Identification of protein oligomerization states by analysis of interface conservation
    • Elcock, A. H., and McCammon, J. A. (2001) Identification of protein oligomerization states by analysis of interface conservation. Proc. Natl. Acad. Sci. U.S.A. 98, 2990-2994.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2990-2994
    • Elcock, A.H.1    McCammon, J.A.2
  • 35
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham, S., and Bowie, J. U. (2002) Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316, 1-6.
    • (2002) J. Mol. Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 36
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali, H., Nollert, P., Royant, A., Menzel, C., Rosenbusch, J. P., Landau, E. M., and Pebay-Peyroula, E. (1999) Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Struct. Folding Des. 7, 909-917.
    • (1999) Struct. Folding Des , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 37
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., and Landau, E. M. (1997) X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. 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
  • 38
    • 0035956936 scopus 로고    scopus 로고
    • Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli
    • Borgnia, M. J., and Agre, P. (2001) Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 98, 2888-2893.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2888-2893
    • Borgnia, M.J.1    Agre, P.2
  • 39
    • 0037036374 scopus 로고    scopus 로고
    • Role of C-terminal domain and transmembrane helices 5 and 6 in function and quaternary structure of major intrinsic proteins: Analysis of aquaporin/glycerol facilitator chimeric proteins
    • Duchesne, L., Pellerin, I., Delamarche, C., Deschamps, S., Lagree, V., Froger, A., Bonnec, G., Thomas, D., and Hubert, J. F. (2002) Role of C-terminal domain and transmembrane helices 5 and 6 in function and quaternary structure of major intrinsic proteins: Analysis of aquaporin/glycerol facilitator chimeric proteins. J. Biol. Chem. 277, 20598-20604.
    • (2002) J. Biol. Chem , vol.277 , pp. 20598-20604
    • Duchesne, L.1    Pellerin, I.2    Delamarche, C.3    Deschamps, S.4    Lagree, V.5    Froger, A.6    Bonnec, G.7    Thomas, D.8    Hubert, J.F.9
  • 45
    • 0025333990 scopus 로고
    • Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-β-D- glucopyranoside and evidence for a tetrameric structure
    • Aerts, T., Xia, J. Z., Siegers, H., de Block, J., and Clauwaert, J. (1990) Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-β-D- glucopyranoside and evidence for a tetrameric structure. J. Biol. Chem. 265, 8675-8680.
    • (1990) J. Biol. Chem , vol.265 , pp. 8675-8680
    • Aerts, T.1    Xia, J.Z.2    Siegers, H.3    de Block, J.4    Clauwaert, J.5
  • 46
    • 0031556944 scopus 로고    scopus 로고
    • Characterisation of the major intrinsic protein (MIP) from bovine lens fibre membranes by electron microscopy and hydrodynamics
    • Konig, N., Zampighi, G. A., and Butler, P. J. (1997) Characterisation of the major intrinsic protein (MIP) from bovine lens fibre membranes by electron microscopy and hydrodynamics. J. Mol. Biol. 265, 590-602.
    • (1997) J. Mol. Biol , vol.265 , pp. 590-602
    • Konig, N.1    Zampighi, G.A.2    Butler, P.J.3
  • 47
    • 0025922827 scopus 로고
    • Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • Smith, B. L., and Agre, P. (1991) Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266, 6407-6415.
    • (1991) J. Biol. Chem , vol.266 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 49
    • 0033522389 scopus 로고    scopus 로고
    • An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus
    • Kamsteeg, E. J., Wormhoudt, T. A., Rijss, J. P., van Os, C. H., and Deen, P. M. (1999) An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. EMBO J. 18, 2394-2400.
    • (1999) EMBO J , vol.18 , pp. 2394-2400
    • Kamsteeg, E.J.1    Wormhoudt, T.A.2    Rijss, J.P.3    van Os, C.H.4    Deen, P.M.5
  • 51
    • 0033520347 scopus 로고    scopus 로고
    • Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
    • Ringler, P., Borgnia, M. J., Stahlberg, H., Maloney, P. C., Agre, P., and Engel, A. (1999) Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography. J. Mol. Biol. 291, 1181-1190.
    • (1999) J. Mol. Biol , vol.291 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Maloney, P.C.4    Agre, P.5    Engel, A.6
  • 52
    • 1542674158 scopus 로고    scopus 로고
    • Preparation of glycerol facilitator for protein structure and folding studies in solution
    • Manley, D., and O'Neil, J. D. (2003) Preparation of glycerol facilitator for protein structure and folding studies in solution. Methods Mol. Biol. 228, 89-101.
    • (2003) Methods Mol. Biol , vol.228 , pp. 89-101
    • Manley, D.1    O'Neil, J.D.2
  • 53
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani, P., Lockless, S. W., Nairn, A. C., and Gadsby, D. C. (2005) CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433, 876-880.
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 54
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
    • (1986) J. Mol. Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 55
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and Walker, J. E. (1996) Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 56
    • 0028078607 scopus 로고
    • Separation of Inner and Outer-Membrane Vesicles from Escherichiacoli in Self-Generating Percoll Gradients
    • Morein, S., Henricson, D., and Rilfors, L. (1994) Separation of Inner and Outer-Membrane Vesicles from Escherichiacoli in Self-Generating Percoll Gradients. Anal. Biochem. 216, 47-51.
    • (1994) Anal. Biochem , vol.216 , pp. 47-51
    • Morein, S.1    Henricson, D.2    Rilfors, L.3
  • 57
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 58
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H., and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 59
    • 0024544308 scopus 로고
    • Adsorption of proteins onto glass surfaces and its effect on the intensity of circular dichroism spectra
    • Wu, C. S., and Chen, G. C. (1989) Adsorption of proteins onto glass surfaces and its effect on the intensity of circular dichroism spectra. Anal. Biochem. 177, 178-182.
    • (1989) Anal. Biochem , vol.177 , pp. 178-182
    • Wu, C.S.1    Chen, G.C.2
  • 60
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A., and Johnson, W. C., Jr. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155, 155-167.
    • (1986) Anal. Biochem , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 61
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 62
    • 25444474165 scopus 로고    scopus 로고
    • Using micellar mole fractions to assess membrane protein stability in mixed micelles
    • Sehgal, P., Mogensen, J. E., and Otzen, D. E. (2005) Using micellar mole fractions to assess membrane protein stability in mixed micelles. Biochim. Biophys. Acta 1716, 59-68.
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 59-68
    • Sehgal, P.1    Mogensen, J.E.2    Otzen, D.E.3
  • 63
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson, A. D., and Murphy, K. P. (1997) Protein structure and the energetics of protein stability. Chem. Rev. 97, 1251-1267.
    • (1997) Chem. Rev , vol.97 , pp. 1251-1267
    • Robertson, A.D.1    Murphy, K.P.2
  • 64
    • 0004149831 scopus 로고    scopus 로고
    • 5th ed, Wolfram Media, Champaign, IL
    • Wolfram, S. (2004) The mathematica book, 5th ed., Wolfram Media, Champaign, IL.
    • (2004) The mathematica book
    • Wolfram, S.1
  • 65
    • 84981976342 scopus 로고
    • Distinguishing transmembrane helices from peripheral helices by circular dichrosim
    • Fasman, G. D. (1993) Distinguishing transmembrane helices from peripheral helices by circular dichrosim. Biotechnol. Appl. Biochem. 18, 111-138.
    • (1993) Biotechnol. Appl. Biochem , vol.18 , pp. 111-138
    • Fasman, G.D.1
  • 68
    • 0025929570 scopus 로고
    • Fluorescence Techniques for Studying Protein Structure
    • Eftink, M. R. (1991) Fluorescence Techniques for Studying Protein Structure. Methods Biochem. Anal. 35, 127-205.
    • (1991) Methods Biochem. Anal , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 69
    • 0034877118 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
    • Reshetnyak, Y. K., Koshevnik, Y., and Burstein, E. A. (2001) Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues. Biophys. J. 81, 1735-1758.
    • (2001) Biophys. J , vol.81 , pp. 1735-1758
    • Reshetnyak, Y.K.1    Koshevnik, Y.2    Burstein, E.A.3
  • 70
    • 3242878900 scopus 로고    scopus 로고
    • Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins
    • Redfield, C. (2004) Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins. Methods 34, 121-132.
    • (2004) Methods , vol.34 , pp. 121-132
    • Redfield, C.1
  • 71
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations
    • Takagi, F., Koga, N., and Takada, S. (2003) How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations. Proc. Natl. Acad. Sci. U.S.A. 100, 11367-11372.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 72
    • 0027410583 scopus 로고
    • Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator
    • Voegele, R. T., Sweet, G. D., and Boos, W. (1993) Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator. J. Bacteriol. 175, 1087-1094.
    • (1993) J. Bacteriol , vol.175 , pp. 1087-1094
    • Voegele, R.T.1    Sweet, G.D.2    Boos, W.3
  • 73
    • 0032885938 scopus 로고    scopus 로고
    • Role of leaflet asymmetry in the permeability of model biological membranes to protons, solutes, and gases
    • Hill, W. G., Rivers, R. L., and Zeidel, M. L. (1999) Role of leaflet asymmetry in the permeability of model biological membranes to protons, solutes, and gases. J. Gen. Physiol. 114, 405-414.
    • (1999) J. Gen. Physiol , vol.114 , pp. 405-414
    • Hill, W.G.1    Rivers, R.L.2    Zeidel, M.L.3
  • 74
    • 29144496893 scopus 로고    scopus 로고
    • Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals
    • Palanivelu, D. V., Kozono, D. E., Engel, A., Suda, K., Lustig, A., Agre, P., and Schirmer, T. (2006) Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals. J. Mol. Biol. 355, 605-611.
    • (2006) J. Mol. Biol , vol.355 , pp. 605-611
    • Palanivelu, D.V.1    Kozono, D.E.2    Engel, A.3    Suda, K.4    Lustig, A.5    Agre, P.6    Schirmer, T.7
  • 75
    • 33751213049 scopus 로고    scopus 로고
    • Spatial organization of the bacterial chemotaxis system
    • Kentner, D., and Sourjik, V. (2006) Spatial organization of the bacterial chemotaxis system. Curr. Opin. Microbiol. 9, 619-624.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 619-624
    • Kentner, D.1    Sourjik, V.2
  • 76
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and Freire, E. (1995) Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys, Acta 1241, 295-322.
    • (1995) Biochim. Biophys, Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 77
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia, T., Semo, N., Arrondo, J. L., Goni, F. M., and Freire, E. (1994) Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33, 9731-9740.
    • (1994) Biochemistry , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.3    Goni, F.M.4    Freire, E.5
  • 78
    • 34250869055 scopus 로고    scopus 로고
    • Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism
    • O'Brien, E. P., Dima, R. I., Brooks, B., and Thirumalai, D. (2007) Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism. J. Am. Chem. Soc. 129, 7346-7353.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 7346-7353
    • O'Brien, E.P.1    Dima, R.I.2    Brooks, B.3    Thirumalai, D.4
  • 79
    • 0035960562 scopus 로고    scopus 로고
    • Dimeric procaspase-3 unfolds via a four-state equilibrium process
    • Bose, K., and Clark, A. C. (2001) Dimeric procaspase-3 unfolds via a four-state equilibrium process. Biochemistry 40, 14236-14242.
    • (2001) Biochemistry , vol.40 , pp. 14236-14242
    • Bose, K.1    Clark, A.C.2
  • 80
    • 18244366077 scopus 로고    scopus 로고
    • Large structure rearrangement of colicin la channel domain after membrane binding from 2D C-13 spin diffusion NMR
    • Luo, W. B., Yao, X. L., and Hong, M. (2005) Large structure rearrangement of colicin la channel domain after membrane binding from 2D C-13 spin diffusion NMR. J. Am. Chem. Soc. 127, 6402-6408.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 6402-6408
    • Luo, W.B.1    Yao, X.L.2    Hong, M.3
  • 81
    • 0035183282 scopus 로고    scopus 로고
    • The mechanism of glycerol conduction in aquaglyceroporins
    • Jensen, M. O., Tajkhorshid, E., and Schulten, K. (2001) The mechanism of glycerol conduction in aquaglyceroporins. Structure 9, 1083-1093.
    • (2001) Structure , vol.9 , pp. 1083-1093
    • Jensen, M.O.1    Tajkhorshid, E.2    Schulten, K.3
  • 82
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • deGroot, B. L., and Grubmuller, H. (2001) Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF. Science 294, 2353-2357.
    • (2001) Science , vol.294 , pp. 2353-2357
    • deGroot, B.L.1    Grubmuller, H.2
  • 83
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wuthrich, K. (1998) TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. U.S.A. 95, 13585-13590.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 84
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: Practice and challenges
    • Sanders, C. R., and Sonnichsen, F. (2006) Solution NMR of membrane proteins: Practice and challenges. Magn. Reson. Chem. 44, S24-S40.
    • (2006) Magn. Reson. Chem , vol.44
    • Sanders, C.R.1    Sonnichsen, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.