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Volumn , Issue SUPPL.53, 2008, Pages

Determination of membrane protein molecular weight using sedimentation equilibrium analytical ultracentrifugation

Author keywords

Analytical ultracentrifugation; Membrane protein; Thermodynamics

Indexed keywords

DETERGENT; MEMBRANE PROTEIN;

EID: 55249091365     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps0712s53     Document Type: Review
Times cited : (27)

References (33)
  • 1
    • 0001473449 scopus 로고
    • Determination of the aggregate size in detergent solution of the lightharvesting chlorophyll a/b-protein complex from chloroplast membranes
    • Butler, P.J. and Kuhlbrandt, W. 1988. Determination of the aggregate size in detergent solution of the lightharvesting chlorophyll a/b-protein complex from chloroplast membranes. Proc. Natl. Acad. Sci. U.S.A. 85:3797-3801.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3797-3801
    • Butler, P.J.1    Kuhlbrandt, W.2
  • 2
    • 3042561938 scopus 로고    scopus 로고
    • The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state
    • Butler, P.J, Ubarretxena-Belandia, I, Warne, T, and Tate, C.G. 2004. The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state. J. Mol. Biol. 340: 797-808.
    • (2004) J. Mol. Biol. , vol.340 , pp. 797-808
    • Butler, P.J.1    Ubarretxena-Belandia, I.2    Warne, T.3    Tate, C.G.4
  • 3
    • 77956752195 scopus 로고
    • Thermodynamic analysis of multicomponent systems
    • Casassa, E.F. and Eisenberg, H. 1964. Thermodynamic analysis of multicomponent systems. Adv. Protein Chem. 19:287-395.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 287-395
    • Casassa, E.F.1    Eisenberg, H.2
  • 4
    • 6344236852 scopus 로고    scopus 로고
    • Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer
    • Doura, A.K. and Fleming, K.G. 2004. Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer. J. Mol. Biol. 343:1487-1497.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1487-1497
    • Doura, A.K.1    Fleming, K.G.2
  • 5
    • 3843102625 scopus 로고    scopus 로고
    • Sequence contextmodulates the stability of a GxxxG mediated transmembrane helix-helix dimer
    • Doura, A.K, Kobus, F.J, Dubrovsky, L, Hibbard, E, and Fleming, K.G. 2004. Sequence contextmodulates the stability of a GxxxG mediated transmembrane helix-helix dimer. J. Mol. Biol. 341:991-998.
    • (2004) J. Mol. Biol. , vol.341 , pp. 991-998
    • Doura, A.K.1    Kobus, F.J.2    Dubrovsky, L.3    Hibbard, E.4    Fleming, K.G.5
  • 6
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • (H.-J. Hinz, ed.) Springer-Verlag, Berlin
    • Durshlag, H. 1986. Specific volumes of biological macromolecules and some other molecules of biological interest. In Thermodynamic Data for Biochemistry and Biotechnology. (H.-J. Hinz, ed.), pp. 45-128. Springer-Verlag, Berlin.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durshlag, H.1
  • 7
    • 33846390316 scopus 로고    scopus 로고
    • Dimerization of the erythropoietin receptor transmembrane domain in micelles
    • Ebie, A.Z. and Fleming, K.G. 2007. Dimerization of the erythropoietin receptor transmembrane domain in micelles. J. Mol. Biol. 366:517-524.
    • (2007) J. Mol. Biol. , vol.366 , pp. 517-524
    • Ebie, A.Z.1    Fleming, K.G.2
  • 9
    • 0000094706 scopus 로고    scopus 로고
    • Measuring transmembrane α-helix energies using analytical ultracentrifugation
    • (J.C. Hanson, ed.) Springer-Verlag, New York
    • Fleming, K.G. 1998. Measuring transmembrane α-helix energies using analytical ultracentrifugation. In Chemtracts: Biological Applications of the Analytical Ultracentrifuge. (J.C. Hanson, ed.), pp. 985-990. Springer-Verlag, New York.
    • (1998) Chemtracts: Biological Applications of the Analytical Ultracentrifuge , pp. 985-990
    • Fleming, K.G.1
  • 10
    • 0034581353 scopus 로고    scopus 로고
    • Probing the stability of helical membrane proteins
    • Fleming, K.G. 2000. Probing the stability of helical membrane proteins. Meth. Enzymol. 323:63-77.
    • (2000) Meth. Enzymol. , vol.323 , pp. 63-77
    • Fleming, K.G.1
  • 11
    • 0036408542 scopus 로고    scopus 로고
    • Standardizing the free energy change of transmembrane helix-helix interactions
    • Fleming, K.G. 2002. Standardizing the free energy change of transmembrane helix-helix interactions. J. Mol. Biol. 323:563-571.
    • (2002) J. Mol. Biol. , vol.323 , pp. 563-571
    • Fleming, K.G.1
  • 12
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane α-helix dimerization
    • Fleming, K.G, Ackerman, A.L, and Engelman, D.M. 1997. The effect of point mutations on the free energy of transmembrane α-helix dimerization. J. Mol. Bio. 272:266-275.
    • (1997) J. Mol. Bio. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 13
    • 0035807810 scopus 로고    scopus 로고
    • Specificity in transmembrane helix-helix interactions defines a hierarchy of stability for sequence variants
    • Fleming, K.G, and Engelman, D.M. 2001. Specificity in transmembrane helix-helix interactions defines a hierarchy of stability for sequence variants. Proc. Natl. Acad. Sci. U.S.A. 98:14340-14344.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14340-14344
    • Fleming, K.G.1    Engelman, D.M.2
  • 14
    • 1642402052 scopus 로고    scopus 로고
    • Thermodynamics of glycophorinAtransmembrane helix-helix association inC14 betainemicelles
    • Fleming, K.G, Ren, C.C, Doura, A.K, Kobus, F.J, Eisley,M.E, and Stanley, A.M. 2004. Thermodynamics of glycophorinAtransmembrane helix-helix association inC14 betainemicelles. Biophys. Chem. 108:43-49.
    • (2004) Biophys. Chem. , vol.108 , pp. 43-49
    • Fleming, K.G.1    Ren, C.C.2    Doura, A.K.3    Kobus, F.J.4    Eisley, M.E.5    Stanley, A.M.6
  • 15
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski, H, Lear, J.D, and DeGrado, W.F. 2001. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. U.S.A. 98:880-885.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    Degrado, W.F.3
  • 16
    • 0037172965 scopus 로고    scopus 로고
    • Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein
    • Howard, K.P, Lear, J.D, and DeGrado, W.F. 2002. Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. Proc. Natl. Acad. Sci. U.S.A. 99:8568-8572.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8568-8572
    • Howard, K.P.1    Lear, J.D.2    Degrado, W.F.3
  • 17
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M.L, Correia, J.J, Yphantis, D.A, and Halvorson, H.R. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 18
    • 13444287923 scopus 로고    scopus 로고
    • The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions
    • Kobus, F.J. and Fleming, K.G. 2005. The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions. Biochemistry 44:1464-1470.
    • (2005) Biochemistry , vol.44 , pp. 1464-1470
    • Kobus, F.J.1    Fleming, K.G.2
  • 19
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
    • Kochendoerfer, G.G, Salom, D, Lear, J.D, Wilk-Orescan, R, Kent, S.B, and DeGrado, W.F. 1999. Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly. Biochemistry 38:11905-11913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    Degrado, W.F.6
  • 20
    • 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
  • 21
    • 0020657411 scopus 로고
    • Mode of interaction of polyoxyethyleneglycol detergents with membrane proteins
    • Le Maire, M, Kwee, K, Anderson, J.P, and Møller, J.V. 1983. Mode of interaction of polyoxyethyleneglycol detergents with membrane proteins. Eur. J. Biochem. 129:525-532.
    • (1983) Eur. J. Biochem. , vol.129 , pp. 525-532
    • Le Maire, M.1    Kwee, K.2    Anderson, J.P.3    Møller, J.V.4
  • 22
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Le Maire, M, Champeil, P, and Møller, J.V. 2000. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508:86-111.
    • (2000) Biochim. Biophys. Acta. , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 23
    • 2942700100 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of Integrin alpha IIb subunit in cell membranes
    • Li, R, Gorelik, R, Nanda, V, Law, P.B, Lear, J.D, DeGrado,W.F, and Bennett, J.S. 2004. Dimerization of the transmembrane domain of Integrin alpha IIb subunit in cell membranes. J. Biol. Chem. 279:26666-26673.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26666-26673
    • Li, R.1    Gorelik, R.2    Nanda, V.3    Law, P.B.4    Lear, J.D.5    DeGrado, W.F.6    Bennett, J.S.7
  • 26
    • 0022293589 scopus 로고
    • Determination of protein molecular weight in complexes with detergent without knowledge of binding
    • Reynolds, J.A. and McCaslin, D.R. 1985. Determination of protein molecular weight in complexes with detergent without knowledge of binding. Meth. Enzymol. 117:41-53.
    • (1985) Meth. Enzymol. , vol.117 , pp. 41-53
    • Reynolds, J.A.1    McCaslin, D.R.2
  • 27
    • 2142856595 scopus 로고
    • Determination of molecular weight of the protein moiety in proteindetergent complexes without direct knowledge of detergent binding
    • Reynolds, J.A, and Tanford, C. 1976. Determination of molecular weight of the protein moiety in proteindetergent complexes without direct knowledge of detergent binding. Proc. Natl. Acad. Sci. U.S.A. 73:4467-4470.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 4467-4470
    • Reynolds, J.A.1    Tanford, C.2
  • 28
    • 14844355538 scopus 로고    scopus 로고
    • The transmembrane domains of the ErbB receptors do not dimerize strongly in micelles
    • Stanley, A.M. and Fleming, K.G. 2005. The transmembrane domains of the ErbB receptors do not dimerize strongly in micelles. J. Mol. Biol. 347:759-772.
    • (2005) J. Mol. Biol. , vol.347 , pp. 759-772
    • Stanley, A.M.1    Fleming, K.G.2
  • 29
    • 34250187443 scopus 로고    scopus 로고
    • The role of a hydrogen bonding network in the transmembrane beta-barrel OMPLA
    • Stanley, A.M. and Fleming, K.G. 2007. The role of a hydrogen bonding network in the transmembrane beta-barrel OMPLA. J. Mol. Biol. 370:912-924.
    • (2007) J. Mol. Biol. , vol.370 , pp. 912-924
    • Stanley, A.M.1    Fleming, K.G.2
  • 30
    • 33645109087 scopus 로고    scopus 로고
    • Energetics of outer membrane phospholipase A (OMPLA) dimerization
    • Stanley, A.M, Chauwang, P, Hendrickson, T.L, and Fleming, K.G. 2006. Energetics of outer membrane phospholipase A (OMPLA) dimerization. J. Mol. Biol. 358:120-131.
    • (2006) J. Mol. Biol. , vol.358 , pp. 120-131
    • Stanley, A.M.1    Chauwang, P.2    Hendrickson, T.L.3    Fleming, K.G.4
  • 32
    • 0021714441 scopus 로고
    • The functional and physical form of mammalian cytochrome c oxidase determined by gel filtration, radiation inactivation, and sedimentation equilibrium analysis
    • Suarez, M.D, Revzin, A, Narlock, R, Kempner, E.S, Thompson, D.A, and Ferguson-Miller, S. 1984. The functional and physical form of mammalian cytochrome c oxidase determined by gel filtration, radiation inactivation, and sedimentation equilibrium analysis. J. Biol. Chem. 259:13791-13799.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13791-13799
    • Suarez, M.D.1    Revzin, A.2    Narlock, R.3    Kempner, E.S.4    Thompson, D.A.5    Ferguson-Miller, S.6
  • 33
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis, D.A. 1964. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 3:297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.