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Volumn 33, Issue 5-6 SPECL.ISSUE, 2007, Pages 399-419

Analytical ultracentrifugation sedimentation velocity for the characterization of detergent-solubilized membrane proteins Ca ++-ATPase and ExbB

Author keywords

Analytical ultracentrifugation; Ca ++ ATPase; ExbB; Membrane proteins

Indexed keywords


EID: 77954615206     PISSN: 00920606     EISSN: 15730689     Source Type: Journal    
DOI: 10.1007/s10867-008-9058-3     Document Type: Article
Times cited : (42)

References (31)
  • 1
    • 5644275289 scopus 로고    scopus 로고
    • Partial specific volume and solvent interactions of amphipol A8-35
    • Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L., Ebel, C.: Partial specific volume and solvent interactions of amphipol A8-35. Anal. Biochem. 334(2), 318-334 (2004)
    • (2004) Anal. Biochem. , vol.334 , Issue.2 , pp. 318-334
    • Gohon, Y.1    Pavlov, G.2    Timmins, P.3    Tribet, C.4    Popot, J.-L.5    Ebel, C.6
  • 2
    • 33750296008 scopus 로고    scopus 로고
    • Lactobionamide surfactants with hydrogenated, perfluorinated or hemifluorinated tails: Physical-chemical and biochemical characterization
    • Lebaupain, F., Salvay, A.G., Olivier, B., Durand, G., Fabiano, A.-S., Michel, N., Popot, J.-L., Ebel, C., Breyton, C., Pucci, B.: Lactobionamide surfactants with hydrogenated, perfluorinated or hemifluorinated tails: physical-chemical and biochemical characterization. Langmuir 22(21), 8881-8890 (2006)
    • (2006) Langmuir , vol.22 , Issue.21 , pp. 8881-8890
    • Lebaupain, F.1    Salvay, A.G.2    Olivier, B.3    Durand, G.4    Fabiano, A.-S.5    Michel, N.6    Popot, J.-L.7    Ebel, C.8    Breyton, C.9    Pucci, B.10
  • 3
    • 0037007002 scopus 로고    scopus 로고
    • Cholate-induced dimerization of detergent-or phospholipid-solubilized bovine cytochrome C oxidase
    • Musatov, A., Robinson, N.C.: Cholate-induced dimerization of detergent-or phospholipid-solubilized bovine cytochrome C oxidase. Biochemistry 41(13), 4371-4376 (2002)
    • (2002) Biochemistry , vol.41 , Issue.13 , pp. 4371-4376
    • Musatov, A.1    Robinson, N.C.2
  • 5
    • 0036408542 scopus 로고    scopus 로고
    • Standardizing the free energy change of transmembrane helix-helix interactions
    • Fleming, K.G.: Standardizing the free energy change of transmembrane helix-helix interactions. J. Mol. Biol. 323, 563-571 (2002)
    • (2002) J. Mol. Biol. , vol.323 , pp. 563-571
    • Fleming, K.G.1
  • 6
    • 0242353821 scopus 로고    scopus 로고
    • Effect of detergents on the association of the glycophorin A transmembrane helix
    • Fisher, L.E., Engelman, D.M., Sturgis, J.N.: Effect of detergents on the association of the glycophorin A transmembrane helix. Biophys. J. 85, 3097-3105 (2003)
    • (2003) Biophys. J. , vol.85 , pp. 3097-3105
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 8
    • 0030845293 scopus 로고    scopus 로고
    • Dimer to monomer conversion of the cytochrome b6 f complex. Causes and consequences
    • Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L.: Dimer to monomer conversion of the cytochrome b6 f complex. Causes and consequences. J. Biol. Chem. 272, 21892-21900 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 21892-21900
    • Breyton, C.1    Tribet, C.2    Olive, J.3    Dubacq, J.-P.4    Popot, J.-L.5
  • 9
    • 10244221042 scopus 로고    scopus 로고
    • Analytical Ultracentrifugation for the study of biological macromolecules
    • Ebel, C.: Analytical Ultracentrifugation for the study of biological macromolecules. Progr. Colloid Polym. Sci. 127, 73-82 (2004)
    • (2004) Progr. Colloid Polym. Sci. , vol.127 , pp. 73-82
    • Ebel, C.1
  • 10
    • 38149020669 scopus 로고    scopus 로고
    • Analytical ultracentrifugation: State of the art and perspectives
    • Uversky, V., Permyakov, E.A. (eds.) Nova Science Publishers, New York
    • Ebel, C.: Analytical ultracentrifugation: State of the art and perspectives. In: Uversky, V., Permyakov, E.A. (eds.) Protein Structures: Methods in Protein Structure and Stability Analysis. Nova Science Publishers, New York (2007)
    • (2007) Protein Structures: Methods in Protein Structure and Stability Analysis
    • Ebel, C.1
  • 12
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modelling
    • Schuck, P.: Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modelling. Biophys. J. 78, 1606-1619 (2000)
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 13
    • 1842428822 scopus 로고    scopus 로고
    • Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles
    • Dam, J., Schuck, P.: Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles. Methods Enzymol. 384, 185-212 (2004)
    • (2004) Methods Enzymol. , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 14
    • 11844290722 scopus 로고    scopus 로고
    • Studying multiprotein complexes by multi-signal sedimentation velocity analytical ultracentrifugation
    • Balbo, A., Minor, K.H., Velikovsky, C.A., Mariuzza, R.A., Peterson, C.B., Schuck, P.: Studying multiprotein complexes by multi-signal sedimentation velocity analytical ultracentrifugation. PNAS 102, 81-86 (2005)
    • (2005) PNAS , vol.102 , pp. 81-86
    • Balbo, A.1    Minor, K.H.2    Velikovsky, C.A.3    Mariuzza, R.A.4    Peterson, C.B.5    Schuck, P.6
  • 16
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Møller, J.V., le Maire, M.: Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J. Biol. Chem. 268(25), 18659-18672 (1993)
    • (1993) J. Biol. Chem. , vol.268 , Issue.25 , pp. 18659-18672
    • Møller, J.V.1    Le Maire, M.2
  • 17
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller, J.V., Juul, B., le Maire, M.: Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286, 1-51 (1996)
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    Le Maire, M.3
  • 20
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle, K., Kadner, R.J.: Touch and go: tying TonB to transport. Mol. Microbiol. 49(4), 869-882 (2003)
    • (2003) Mol. Microbiol. , vol.49 , Issue.4 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 21
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs, P.I., Larsen, R.A., Postle, K.: Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol. Microbiol. 44(1), 271-281 (2002)
    • (2002) Mol. Microbiol. , vol.44 , Issue.1 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 22
    • 0036723874 scopus 로고    scopus 로고
    • ExbB and ExbD do not function independently in TonB-dependent energy transduction
    • Held, K.G., Postle, K.: ExbB and ExbD do not function independently in TonB-dependent energy transduction. J. Bacteriol. 184, 5170-5173 (2002)
    • (2002) J. Bacteriol. , vol.184 , pp. 5170-5173
    • Held, K.G.1    Postle, K.2
  • 23
    • 33750293579 scopus 로고    scopus 로고
    • Analytical ultracentrifuge for the characterization of detergent in solution
    • Salvay, A.G., Ebel, C.: Analytical ultracentrifuge for the characterization of detergent in solution. Progr. Colloid Polym. Sci. 131, 74-82 (2006)
    • (2006) Progr. Colloid Polym. Sci. , vol.131 , pp. 74-82
    • Salvay, A.G.1    Ebel, C.2
  • 24
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • Hayashi, Y., Matsui, H., Takagi, T.: Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography. Methods Enzymol. 172, 514-525 (1989)
    • (1989) Methods Enzymol. , vol.172 , pp. 514-525
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 25
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the Glutamate Transporters from Bacillus caldotenax and bacillus stearothermophilus
    • Yernool, D., Boudker, O., Folta-Stogniew, E., Gouaux, E.: Trimeric subunit stoichiometry of the Glutamate Transporters from Bacillus caldotenax and bacillus stearothermophilus. Biochemistry 42, 12981-12988 (2003)
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4
  • 26
    • 23144459878 scopus 로고    scopus 로고
    • Linear and non-linear pressure dependence of enzyme catalytic parameters
    • Masson, P., Balny, C.: Linear and non-linear pressure dependence of enzyme catalytic parameters. Biochim. Biophys. Acta 1724, 440-450 (2005)
    • (2005) Biochim. Biophys. Acta , vol.1724 , pp. 440-450
    • Masson, P.1    Balny, C.2
  • 27
    • 0343023273 scopus 로고
    • Micelle formation of cationic detergent solution at high pressures
    • Osugi, J., Sato, M., Ifuki, N.: Micelle formation of cationic detergent solution at high pressures. The Review of Physical Chemistry of Japan 35(1), 32-37 (1965)
    • (1965) The Review of Physical Chemistry of Japan , vol.35 , Issue.1 , pp. 32-37
    • Osugi, J.1    Sato, M.2    Ifuki, N.3
  • 29
    • 33846925043 scopus 로고    scopus 로고
    • Protein-protein contacts in solubilized membrane proteins, as detected by cross-linking
    • le Maire, M., Møller, J.V., Menguy, T., Velours, J., Champeil, P.: Protein-protein contacts in solubilized membrane proteins, as detected by cross-linking. Anal. Biochem. 362, 168-171 (2007)
    • (2007) Anal. Biochem. , vol.362 , pp. 168-171
    • Le Maire, M.1    Møller, J.V.2    Menguy, T.3    Velours, J.4    Champeil, P.5
  • 31
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled-receptor as a functional unit
    • Chabre, M., le Maire, M.: Monomeric G-protein-coupled-receptor as a functional unit. Biochemistry 44, 9395-9403 (2005)
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    Le Maire, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.