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Volumn 334, Issue 2, 2004, Pages 318-334

Partial specific volume and solvent interactions of amphipol A8-35

Author keywords

Amphipol; Analytical ultracentrifugation; Counter ion dissociation; Density; Polyelectrolyte; Small angle neutron scattering

Indexed keywords

BUOYANCY; CARBOXYLATION; DENSITY (SPECIFIC GRAVITY); DISSOCIATION; ION EXCHANGE; MOLAR RATIO; POLYELECTROLYTES; PROTEINS;

EID: 5644275289     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.07.033     Document Type: Article
Times cited : (88)

References (41)
  • 2
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • J.U. Bowie Stabilizing membrane proteins Curr. Opin. Struct. Biol. 11 2001 397 402
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 6
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • C. Tribet, R. Audebert, and J.-L. Popot Amphipols: polymers that keep membrane proteins soluble in aqueous solutions Proc. Natl. Acad. Sci. USA 93 1996 15047 15050
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 10
    • 0037174145 scopus 로고    scopus 로고
    • Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints
    • K.L. Martinez, Y. Gohon, P-J. Corringer, C. Tribet, F. Merola, J-P. Changeux, and J.-L. Popot Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints FEBS Lett. 528 2002 251 256
    • (2002) FEBS Lett. , vol.528 , pp. 251-256
    • Martinez, K.L.1    Gohon, Y.2    Corringer, P.-J.3    Tribet, C.4    Merola, F.5    Changeux, J.-P.6    Popot, J.-L.7
  • 12
    • 0019562446 scopus 로고
    • Forward scattering of light, X-rays and neutrons
    • H. Eisenberg Forward scattering of light, X-rays and neutrons Q. Rev. Biophys. 14 1981 141 172
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 141-172
    • Eisenberg, H.1
  • 13
    • 0028076138 scopus 로고
    • Protein and nucleic acid hydration and cosolvent interactions: Establishment of reliable baseline values at high cosolvent concentrations
    • H. Eisenberg Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable baseline values at high cosolvent concentrations Biophys. Chem. 53 1994 57 68
    • (1994) Biophys. Chem. , vol.53 , pp. 57-68
    • Eisenberg, H.1
  • 14
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • S.N. Timasheff The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22 1993 67 97
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 15
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • S.N. Timasheff Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated Adv. Protein Chem. 51 1998 355 432
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 18
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • T. Arakawa, and S.N. Timasheff Preferential interactions of proteins with salts in concentrated solutions Biochemistry 21 1982 6545 6552
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 19
    • 0001462245 scopus 로고    scopus 로고
    • Determination of partial molal volumes, and salt and water binding of highly charged biological macromolecules (tRNA, halophilic protein) in multimolar salt solutions
    • B. Kernel, G. Zaccai, and C. Ebel Determination of partial molal volumes, and salt and water binding of highly charged biological macromolecules (tRNA, halophilic protein) in multimolar salt solutions Progr. Colloid. Polym. Sci. 113 1999 168 175
    • (1999) Progr. Colloid. Polym. Sci. , vol.113 , pp. 168-175
    • Kernel, B.1    Zaccai, G.2    Ebel, C.3
  • 23
    • 0034607357 scopus 로고    scopus 로고
    • Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle
    • A. Lustig, A. Engel, G. Tsiotis, E.M. Landau, and W. Baschong Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle Biochim. Biophys. Acta 1464 2000 199 206
    • (2000) Biochim. Biophys. Acta , vol.1464 , pp. 199-206
    • Lustig, A.1    Engel, A.2    Tsiotis, G.3    Landau, E.M.4    Baschong, W.5
  • 24
  • 25
    • 33947090431 scopus 로고
    • Stereospecific and stereoselective reactions. I. Preparation of amines from alcohols
    • O. Mitsunobu, M. Wada, and T. Sano Stereospecific and stereoselective reactions. I. Preparation of amines from alcohols J. Am. Chem. Soc. 94 1972 679 680
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 679-680
    • Mitsunobu, O.1    Wada, M.2    Sano, T.3
  • 26
    • 0024135498 scopus 로고
    • Viscometric behaviour of hydrophobically modified poly(sodium acrylate)
    • K.T. Wang, I. Iliopoulos, and R. Audebert Viscometric behaviour of hydrophobically modified poly(sodium acrylate) Polym. Bull. 20 1988 577 582
    • (1988) Polym. Bull. , vol.20 , pp. 577-582
    • Wang, K.T.1    Iliopoulos, I.2    Audebert, R.3
  • 29
    • 0042860033 scopus 로고    scopus 로고
    • Conformation of heparin studied with macromolecular hydrodynamic methods and X-ray scattering
    • G. Pavlov, S. Finet, K. Tatarenko, E. Korneeva, and C. Ebel Conformation of heparin studied with macromolecular hydrodynamic methods and X-ray scattering Eur. Biophys. J. 32 2003 437 449
    • (2003) Eur. Biophys. J. , vol.32 , pp. 437-449
    • Pavlov, G.1    Finet, S.2    Tatarenko, K.3    Korneeva, E.4    Ebel, C.5
  • 30
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 31
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • P. Schuck, M.A. Perugini, N.R. Gonzales, G.J. Howlett, and D. Schubert Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys. J. 82 2002 1096 1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 32
    • 0033179805 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of interference optical data by systematic noise decomposition
    • P. Schuck Sedimentation equilibrium analysis of interference optical data by systematic noise decomposition Anal. Biochem. 272 1999 199 208
    • (1999) Anal. Biochem. , vol.272 , pp. 199-208
    • Schuck, P.1
  • 33
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • P. Schuck Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation Biophys. J. 75 1998 1503 1512
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 34
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • B. Jacrot, and G. Zaccai Determination of molecular weight by neutron scattering Biopolymers 20 1981 2413 2426
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 35
    • 5644238150 scopus 로고
    • Sedimentation analysis of membrane proteins
    • S.E. Harding A.J. Rowe J.C. Horton The Royal Society of Chemistry Cambridge
    • G.J. Howlett Sedimentation analysis of membrane proteins S.E. Harding A.J. Rowe J.C. Horton Analytical Ultracentrifugation in Biochemistry and Polymer Science 1992 The Royal Society of Chemistry Cambridge 470 483
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 470-483
    • Howlett, G.J.1
  • 36
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • J. Lebowitz, M.S. Lewis, and P. Schuck Modern analytical ultracentrifugation in protein science: a tutorial review Protein Sci. 11 2002 2067 2079
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 37
    • 0043166158 scopus 로고    scopus 로고
    • Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching
    • D. Noy, J.R. Calhoun, and J.D. Lear Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching Anal. Biochem. 320 2003 185 192
    • (2003) Anal. Biochem. , vol.320 , pp. 185-192
    • Noy, D.1    Calhoun, J.R.2    Lear, J.D.3
  • 38
    • 0014216034 scopus 로고
    • The simultaneous determination of partial specific volumes and molecular weights with microgram quantities
    • S.J. Edelstein, and H.K. Schachman The simultaneous determination of partial specific volumes and molecular weights with microgram quantities J. Biol. Chem. 242 1967 306 311
    • (1967) J. Biol. Chem. , vol.242 , pp. 306-311
    • Edelstein, S.J.1    Schachman, H.K.2
  • 40
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • H.-J. Hinz Springer New York
    • H. Durchschlag Specific volumes of biological macromolecules and some other molecules of biological interest H.-J. Hinz Thermodynamic Data for Biochemistry and Biotechnology 1986 Springer New York 45 128
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1
  • 41
    • 0000958543 scopus 로고
    • Biophysics-Nucleic Acids
    • W. Saenger Springer Berlin
    • H. Eisenberg W. Saenger Biophysics-Nucleic Acids Landolt-Bornstein New Series 1990 Springer Berlin 257 276
    • (1990) Landolt-Bornstein New Series , pp. 257-276
    • Eisenberg, H.1


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