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Volumn 108, Issue 1-3, 2004, Pages 89-100

Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: Theory and application to concentrated solutions of ribonuclease

Author keywords

Reversible association; Ribonuclease; Thermodynamic nonideality

Indexed keywords

BUFFER; OLIGOMER; PHOSPHATE; PROTEIN; RIBONUCLEASE; RIBONUCLEASE A;

EID: 1642285049     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2003.10.012     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 0025169221 scopus 로고
    • Quantitative characterization of reversible molecular associations via analytical ultracentrifugation
    • Minton A. Quantitative characterization of reversible molecular associations via analytical ultracentrifugation. Anal. Biochem. 190:1990;1-6.
    • (1990) Anal. Biochem. , vol.190 , pp. 1-6
    • Minton, A.1
  • 2
    • 0032750872 scopus 로고    scopus 로고
    • Characterization of heterologous protein-protein interactions using analytical ultracentrifugation
    • Rivas G., Stafford W., Minton A. Characterization of heterologous protein-protein interactions using analytical ultracentrifugation. Methods. 19:1999;194-212.
    • (1999) Methods , vol.19 , pp. 194-212
    • Rivas, G.1    Stafford, W.2    Minton, A.3
  • 3
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton A.B. How crowded is the cytoplasm? Cell. 30:1982;345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 4
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman S.B., Minton A.P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22:1993;27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 5
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • Minton A.P. Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers. 20:1981;2093-2120.
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 6
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26:2001;597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 7
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276:2001;10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 8
    • 0029841451 scopus 로고    scopus 로고
    • Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism
    • Knull H., Minton A.P. Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism. Cell Biochem. Funct. 14:1996;237-248.
    • (1996) Cell Biochem. Funct. , vol.14 , pp. 237-248
    • Knull, H.1    Minton, A.P.2
  • 9
    • 0033804074 scopus 로고    scopus 로고
    • Analysis of sedimentation equilibrium distributions reflecting nonideal macromolecular associations
    • Wills P., Jacobsen M., Winzor D. Analysis of sedimentation equilibrium distributions reflecting nonideal macromolecular associations. Biophys. J. 79:2000;2178-2187.
    • (2000) Biophys. J. , vol.79 , pp. 2178-2187
    • Wills, P.1    Jacobsen, M.2    Winzor, D.3
  • 10
    • 0034666656 scopus 로고    scopus 로고
    • Analysis of protein self-association under conditions of the thermodynamic non-ideality
    • Behlke J., Ristau O. Analysis of protein self-association under conditions of the thermodynamic non-ideality. Biophys. Chem. 87:2000;1-13.
    • (2000) Biophys. Chem. , vol.87 , pp. 1-13
    • Behlke, J.1    Ristau, O.2
  • 11
    • 0035942981 scopus 로고    scopus 로고
    • Studies of solute self-association by sedimentation equilibrium: Allowance for effects of thermodynamic non-ideality beyond the consequences of nearest-neighbor interactions
    • Wills P., Winzor D. Studies of solute self-association by sedimentation equilibrium: allowance for effects of thermodynamic non-ideality beyond the consequences of nearest-neighbor interactions. Biophys. Chem. 91:2001;253-262.
    • (2001) Biophys. Chem. , vol.91 , pp. 253-262
    • Wills, P.1    Winzor, D.2
  • 12
    • 0023322946 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins
    • Chatelier R.C., Minton A.P. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins. Biopolymers. 26:1987;507-524.
    • (1987) Biopolymers , vol.26 , pp. 507-524
    • Chatelier, R.C.1    Minton, A.P.2
  • 13
    • 0023369557 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components
    • Chatelier R.C., Minton A.P. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components. Biopolymers. 26:1987;1097-1113.
    • (1987) Biopolymers , vol.26 , pp. 1097-1113
    • Chatelier, R.C.1    Minton, A.P.2
  • 14
    • 0033587619 scopus 로고    scopus 로고
    • Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: Theory, experiment, and biological significance
    • Rivas G., Fernández J.A., Minton A.P. Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. Biochemistry. 38:1999;9379-9388.
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernández, J.A.2    Minton, A.P.3
  • 15
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • Minton A.P. The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol. Cell. Biochem. 55:1983;119-140.
    • (1983) Mol. Cell. Biochem. , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 16
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semi-quantitative successes, quantitative challenges'
    • Hall D.R., Minton A.P. Macromolecular crowding: qualitative and semi-quantitative successes, quantitative challenges'. Biochim. Biophys. Acta. 1649:2003;127-139.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 127-139
    • Hall, D.R.1    Minton, A.P.2
  • 17
    • 0035853141 scopus 로고    scopus 로고
    • Direct observation of the enhancement of non-cooperative protein assembly by macromolecular crowding: Indefinite self-association of the bacterial cell division protein FtsZ
    • Rivas G., Fernández J.A., Minton A.P. Direct observation of the enhancement of non-cooperative protein assembly by macromolecular crowding: indefinite self-association of the bacterial cell division protein FtsZ. Proc. Natl. Acad. Sci. USA. 98:2001;3150-3155.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3150-3155
    • Rivas, G.1    Fernández, J.A.2    Minton, A.P.3
  • 18
    • 0024642066 scopus 로고
    • Hidden self-association of proteins
    • Muramatsu N., Minton A.P. Hidden self-association of proteins. J. Mol. Recog. 1:1989;166-171.
    • (1989) J. Mol. Recog. , vol.1 , pp. 166-171
    • Muramatsu, N.1    Minton, A.P.2
  • 19
    • 0034672724 scopus 로고    scopus 로고
    • Analytical ultracentrifugation in a Gibbsian perspective
    • Eisenberg H. Analytical ultracentrifugation in a Gibbsian perspective. Biophys. Chem. 88:2000;1-9.
    • (2000) Biophys. Chem. , vol.88 , pp. 1-9
    • Eisenberg, H.1
  • 20
    • 0003300676 scopus 로고    scopus 로고
    • Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium
    • Minton A.P. Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium. Prog. Colloid Polym. Sci. 107:1997;11-19.
    • (1997) Prog. Colloid Polym. Sci. , vol.107 , pp. 11-19
    • Minton, A.P.1
  • 22
    • 23544458810 scopus 로고
    • The statistical thermodynamics of multicomponent systems
    • McMillan W.G. Jr., Mayer J.E. The statistical thermodynamics of multicomponent systems. J. Chem. Phys. 13:1945;276-305.
    • (1945) J. Chem. Phys. , vol.13 , pp. 276-305
    • Mcmillan Jr., W.G.1    Mayer, J.E.2
  • 23
    • 0015829813 scopus 로고
    • Theory of aggregation in solution. I. General equations and application to the stacking of bases, nucleotides, etc
    • Hill T.L., Chen Y.D. Theory of aggregation in solution. I. General equations and application to the stacking of bases, nucleotides, etc. Biopolymers. 12:1971;1285-1312.
    • (1971) Biopolymers , vol.12 , pp. 1285-1312
    • Hill, T.L.1    Chen, Y.D.2
  • 24
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • Minton A.P. Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol. 206:1998;127-149.
    • (1998) Methods Enzymol. , vol.206 , pp. 127-149
    • Minton, A.P.1
  • 27
    • 77956909282 scopus 로고
    • P.D. Boyer. New York: Academic Press
    • Richards F.M., Wyckoff H.W. Boyer P.D. The Enzymes. 1971;647-806 Academic Press, New York.
    • (1971) The Enzymes , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.W.2
  • 28
    • 0027410312 scopus 로고
    • Rapid and accurate microfractionation of the contents of small centrifuge tubes: Application in the measurement of molecular weights of proteins via sedimentation equilibrium
    • Darawshe S., Rivas G., Minton A.P. Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weights of proteins via sedimentation equilibrium. Anal. Biochem. 209:1993;130-135.
    • (1993) Anal. Biochem. , vol.209 , pp. 130-135
    • Darawshe, S.1    Rivas, G.2    Minton, A.P.3
  • 29
  • 30
    • 0015884463 scopus 로고
    • Concerted formation of the gel of HbS
    • Williams R. Jr. Concerted formation of the gel of HbS. Proc. Natl. Acad. Sci. USA. 70:1973;1506-1508.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1506-1508
    • Williams Jr., R.1
  • 31
    • 0015851091 scopus 로고
    • Effects of pH, 2,3-DPG and salts on gelation of sickle cell deoxyhemoglobin
    • Briehl R., Ewert S. Effects of pH, 2,3-DPG and salts on gelation of sickle cell deoxyhemoglobin. J. Mol. Biol. 80:1973;445-458.
    • (1973) J. Mol. Biol. , vol.80 , pp. 445-458
    • Briehl, R.1    Ewert, S.2
  • 32
    • 0018175121 scopus 로고
    • Temperature dependence of nonideality in concentrated solutions of hemoglobin
    • Ross P.D., Briehl R.W., Minton A.P. Temperature dependence of nonideality in concentrated solutions of hemoglobin. Biopolymers. 17:1978;2285-2288.
    • (1978) Biopolymers , vol.17 , pp. 2285-2288
    • Ross, P.D.1    Briehl, R.W.2    Minton, A.P.3
  • 33
    • 0019764210 scopus 로고
    • Self-association in highly concentrated solutions of myoglobin: A novel analysis of sedimentation equilibrium of highly nonideal solutions
    • Minton A.P., Lewis M.S. Self-association in highly concentrated solutions of myoglobin: a novel analysis of sedimentation equilibrium of highly nonideal solutions. Biophys. Chem. 14:1981;317-324.
    • (1981) Biophys. Chem. , vol.14 , pp. 317-324
    • Minton, A.P.1    Lewis, M.S.2
  • 34
    • 0017381152 scopus 로고
    • Analysis of nonideal behavior in concentrated hemoglobin solutions
    • Ross P., Minton A. Analysis of nonideal behavior in concentrated hemoglobin solutions. J. Mol. Biol. 112:1977;437-452.
    • (1977) J. Mol. Biol. , vol.112 , pp. 437-452
    • Ross, P.1    Minton, A.2
  • 35
    • 0032584210 scopus 로고    scopus 로고
    • The crystal structure of a 3D domain-swapped dimer of RNase a at a 2.1 a resolution
    • Liu Y., Hart P., Schlunegger M., Eisenberg D. The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1 A resolution. Proc. Natl. Acad. Sci. USA. 95:1998;3437-3442.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3437-3442
    • Liu, Y.1    Hart, P.2    Schlunegger, M.3    Eisenberg, D.4
  • 36
    • 0033773675 scopus 로고    scopus 로고
    • Dimer formation by a 'monomeric' protein
    • Park C., Raines R. Dimer formation by a 'monomeric' protein. Protein Sci. 9:2000;2026-2033.
    • (2000) Protein Sci. , vol.9 , pp. 2026-2033
    • Park, C.1    Raines, R.2


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