메뉴 건너뛰기




Volumn 17, Issue 5, 2004, Pages 408-416

Fluorescence anisotropy as a probe to study tracer proteins in crowded solutions

Author keywords

Apparent equilibrium constants; Crowding; Fluorescence anisotropy; Molecular cavities; Rotational diffusion; Rotational viscosity; Time resolved fluorescence

Indexed keywords

1-ANILINO-8-NAPHTHALENESULFONATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; APOMYOGLOBIN; APOPROTEIN; FLUORESCENT DYE; MYOGLOBIN; PANCREATIC RIBONUCLEASE; WATER;

EID: 4544387972     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.712     Document Type: Conference Paper
Times cited : (17)

References (49)
  • 1
    • 0023279461 scopus 로고
    • Protein structure probed by polarization spectroscopy II: A time-resolved fluorescence study of human fibrinogen
    • Acun̄a AU, González-Rodriguez J, Lillo MP, Naqvi R. 1987. Protein structure probed by polarization spectroscopy II: a time-resolved fluorescence study of human fibrinogen. Biophys. Chem. 26: 63-70.
    • (1987) Biophys. Chem. , vol.26 , pp. 63-70
    • Acuna, A.U.1    González-Rodriguez, J.2    Lillo, M.P.3    Naqvi, R.4
  • 2
    • 0014440193 scopus 로고
    • Fluorescence polarization of the complexes of 1-anilino-8- naphthalenesulfonate with bovine serum albumin: Evidence for preferential orientation of the ligand
    • Anderson SR, Weber G. 1969. Fluorescence polarization of the complexes of 1-anilino-8-naphthalenesulfonate with bovine serum albumin: evidence for preferential orientation of the ligand. Biochemistry 8: 371-377.
    • (1969) Biochemistry , vol.8 , pp. 371-377
    • Anderson, S.R.1    Weber, G.2
  • 3
    • 0018407386 scopus 로고
    • Time-resolved fluorescence measurements
    • Badea M, Brand L. 1979. Time-resolved fluorescence measurements. Meth. Enzymol. 61: 378-425.
    • (1979) Meth. Enzymol. , vol.61 , pp. 378-425
    • Badea, M.1    Brand, L.2
  • 4
    • 0034423297 scopus 로고    scopus 로고
    • Observing proteins in their natural habitat: The living cell
    • Bastiaens PI, Pepperkok R. 2000. Observing proteins in their natural habitat: the living cell. Trends Biochem. Sci. 25: 631-637.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 631-637
    • Bastiaens, P.I.1    Pepperkok, R.2
  • 6
    • 0031015166 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a tool to investigate protein interactions
    • Brown MP, Royer C. 1997. Fluorescence spectroscopy as a tool to investigate protein interactions. Curr. Opin. Biotechnol. 8: 45-49.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 45-49
    • Brown, M.P.1    Royer, C.2
  • 7
    • 0023741086 scopus 로고
    • Anisotropy decay as an experimental approach to protein dynamics
    • Bucci E, Steiner RF. 1988. Anisotropy decay as an experimental approach to protein dynamics. Biophys. Chem. 30: 199-224.
    • (1988) Biophys. Chem. , vol.30 , pp. 199-224
    • Bucci, E.1    Steiner, R.F.2
  • 9
    • 0004240239 scopus 로고
    • The Chemical Catalogue Company: New York
    • Debye P. 1929. Polar Molecules. The Chemical Catalogue Company: New York.
    • (1929) Polar Molecules
    • Debye, P.1
  • 10
    • 0000304006 scopus 로고
    • Determination of molecular weight and diffusion coefficients in the ultracentrifuge
    • Ehrenberg A. 1957. Determination of molecular weight and diffusion coefficients in the ultracentrifuge. Acta Chem. Scand. 11: 1257-1270.
    • (1957) Acta Chem. Scand. , vol.11 , pp. 1257-1270
    • Ehrenberg, A.1
  • 11
    • 84976701037 scopus 로고
    • On the theory of the Brownian movement
    • Einstein A. 1906. On the theory of the Brownian movement. Ann. Phys. (Leipzig) 19: 371-381.
    • (1906) Ann. Phys. (Leipzig) , vol.19 , pp. 371-381
    • Einstein, A.1
  • 13
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but under-appreciated
    • Ellis RJ. 2001. Macromolecular crowding: obvious but under-appreciated. Trends Biochem. Sci. 26: 597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 14
    • 0035041251 scopus 로고    scopus 로고
    • The conformation of serum albumin in solution: A combined phosphorescence depolarization - Hydrodynamic modelling study
    • Ferrer ML, Duchowicz R, Carrasco B, García de la Torre J, Acun̄a AU. 2001. The conformation of serum albumin in solution: a combined phosphorescence depolarization - hydrodynamic modelling study. Biophys. J. 80: 2422-2430.
    • (2001) Biophys. J. , vol.80 , pp. 2422-2430
    • Ferrer, M.L.1    Duchowicz, R.2    Carrasco, B.3    García De La Torre, J.4    Acuna, A.U.5
  • 15
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton AB. 1982. How crowded is the cytoplasm? Cell 30: 345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 20
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • Jameson DM, Sawyer WH. 1995. Fluorescence anisotropy applied to biomolecular interactions. Meth. Enzymol. 246: 283-300.
    • (1995) Meth. Enzymol. , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 21
    • 0032743022 scopus 로고    scopus 로고
    • Quantification of protein-protein interactions using fluorescence polarization
    • Jameson DM, Seifried SE. 1999. Quantification of protein-protein interactions using fluorescence polarization. Methods 19: 222-233.
    • (1999) Methods , vol.19 , pp. 222-233
    • Jameson, D.M.1    Seifried, S.E.2
  • 22
    • 0037279631 scopus 로고    scopus 로고
    • Fluorescence: Basic concepts, practical aspects, and some anecdotes
    • Jameson DM, Croney JC, Moens PD. 2003. Fluorescence: basic concepts, practical aspects, and some anecdotes. Meth. Enzymol. 360: 1-43.
    • (2003) Meth. Enzymol. , vol.360 , pp. 1-43
    • Jameson, D.M.1    Croney, J.C.2    Moens, P.D.3
  • 23
    • 0030070010 scopus 로고    scopus 로고
    • Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein
    • Kirk WR, Kurian E, Prendergast FG. 1996. Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys. J. 70: 69-83.
    • (1996) Biophys. J. , vol.70 , pp. 69-83
    • Kirk, W.R.1    Kurian, E.2    Prendergast, F.G.3
  • 25
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis D, Lovrien R. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74: 422-429.
    • (1998) Biophys. J. , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 26
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP. 2000. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10: 34-39.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 27
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton AP. 2001. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276: 10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 28
    • 0037048367 scopus 로고    scopus 로고
    • Caging ultrafast proton transfer and twisting motion of 1-hidroxi-2-acetonaphtona
    • Organero JA, Tormo L, Douhal A. 2002. Caging ultrafast proton transfer and twisting motion of 1-hidroxi-2-acetonaphtona. Chem. Phys. Lett. 363: 409-414.
    • (2002) Chem. Phys. Lett. , vol.363 , pp. 409-414
    • Organero, J.A.1    Tormo, L.2    Douhal, A.3
  • 29
    • 0032079008 scopus 로고    scopus 로고
    • Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments
    • Record TM Jr, Courtenay ES, Cayley S, Gutman HJ. 1998. Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments. Trends Biochem. Sci. 23: 190-194.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 190-194
    • Record Jr., T.M.1    Courtenay, E.S.2    Cayley, S.3    Gutman, H.J.4
  • 30
    • 0037470574 scopus 로고    scopus 로고
    • Effect of dextran on protein stability and conformation attributed to macromolecular crowding
    • Sasahara K, McPhie P, Minton AP. 2003. Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J. Mol. Biol. 326: 1227-1237.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1227-1237
    • Sasahara, K.1    McPhie, P.2    Minton, A.P.3
  • 31
    • 0002276429 scopus 로고
    • The influence of Brownian movement on the viscosity of solutions
    • Simha R. 1940. The influence of Brownian movement on the viscosity of solutions. J. Phys. Chem. 44: 25-34.
    • (1940) J. Phys. Chem. , vol.44 , pp. 25-34
    • Simha, R.1
  • 32
    • 0020480481 scopus 로고
    • Anilinonaphthalene sulfonate as a probe of membrane composition and function
    • Slavik J. 1982. Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim. Biophys. Acta 694: 1-25.
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 1-25
    • Slavik, J.1
  • 33
    • 0017413916 scopus 로고
    • Hydrodynamic of a rigid molecule: Rotational and linear diffusion and fluorescence anisotropy
    • Small EW, Isenberg I. 1977. Hydrodynamic of a rigid molecule: rotational and linear diffusion and fluorescence anisotropy. Biopolymers 16: 1907-1928.
    • (1977) Biopolymers , vol.16 , pp. 1907-1928
    • Small, E.W.1    Isenberg, I.2
  • 35
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of nonpolar binding sites
    • Stryer L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of nonpolar binding sites. J. Mol. Biol. 13: 482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 36
    • 84984085914 scopus 로고
    • Time-dependent fluorescence depolarization and Brownian rotational diffusion of macromolecules
    • Tao T. 1969. Time-dependent fluorescence depolarization and Brownian rotational diffusion of macromolecules. Biopolymers 8: 609-632.
    • (1969) Biopolymers , vol.8 , pp. 609-632
    • Tao, T.1
  • 37
    • 0034701060 scopus 로고    scopus 로고
    • Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins
    • Tcherkasskaya O, Ptitsyn OB, Knutson JR. 2000. Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry 39: 1879-1889.
    • (2000) Biochemistry , vol.39 , pp. 1879-1889
    • Tcherkasskaya, O.1    Ptitsyn, O.B.2    Knutson, J.R.3
  • 40
    • 0036164351 scopus 로고    scopus 로고
    • Solute and macromolecule diffusion in cellular aqueous compartments
    • Verkman AS. 2002. Solute and macromolecule diffusion in cellular aqueous compartments. Trends Biochem. Sci. 27: 27-33.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 27-33
    • Verkman, A.S.1
  • 41
    • 0003157931 scopus 로고
    • Analysis of fluorescence anisotropy decays by a least square method
    • Wahl P. 1979. Analysis of fluorescence anisotropy decays by a least square method. Biophys. Chem. 10: 91-104.
    • (1979) Biophys. Chem. , vol.10 , pp. 91-104
    • Wahl, P.1
  • 42
    • 0005085068 scopus 로고
    • Fluorescence anisotropy decay and Brownian rotational motion: Theory and application in biological systems
    • Cundall RB, Dale RE (eds). NATO ASI Series. Series A: Life Sciences, Plenum Press: New York
    • Wahl P. 1983. Fluorescence anisotropy decay and Brownian rotational motion: theory and application in biological systems. In Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology, Cundall RB, Dale RE (eds). NATO ASI Series. Series A: Life Sciences, Vol. 69; Plenum Press: New York; 497-521.
    • (1983) Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology , vol.69 , pp. 497-521
    • Wahl, P.1
  • 43
    • 0030782485 scopus 로고    scopus 로고
    • Myoglobin and hemoglobin rotational diffusion in the cell
    • Wang D, Kreutzer U, Chung Y, Jue T. 1997. Myoglobin and hemoglobin rotational diffusion in the cell. Biophys. J. 73: 2764-2770.
    • (1997) Biophys. J. , vol.73 , pp. 2764-2770
    • Wang, D.1    Kreutzer, U.2    Chung, Y.3    Jue, T.4
  • 44
    • 76949127690 scopus 로고
    • Polarization of the fluorescence of macromolecules I: Theory and experimental method
    • Weber G. 1952. Polarization of the fluorescence of macromolecules I: theory and experimental method. Biochem. J. 51: 145-155.
    • (1952) Biochem. J. , vol.51 , pp. 145-155
    • Weber, G.1
  • 45
    • 0019890347 scopus 로고
    • Evidence for protein self-association induced by excluded volume: Myoglobin in the presence of globular proteins
    • Wilf J, Minton AP. 1981. Evidence for protein self-association induced by excluded volume: myoglobin in the presence of globular proteins. Biochim. Biophys. Acta 670: 316-322.
    • (1981) Biochim. Biophys. Acta , vol.670 , pp. 316-322
    • Wilf, J.1    Minton, A.P.2
  • 46
    • 0015438669 scopus 로고
    • Nanosecond fluorescence spectroscopy of macromolecules
    • Yguerabide J. 1972. Nanosecond fluorescence spectroscopy of macromolecules. Meth. Enzymol. 26C: 498-578.
    • (1972) Meth. Enzymol. , vol.26 C , pp. 498-578
    • Yguerabide, J.1
  • 47
    • 4544321668 scopus 로고    scopus 로고
    • Protein self-association in crowded protein solutions: A time-resolved fluorescence polarization study
    • in press
    • Zorrilla S, Rivas G, Acuña AU, Lillo MP. 2004a. Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study. Protein Sci. (in press).
    • (2004) Protein Sci.
    • Zorrilla, S.1    Rivas, G.2    Acuña, A.U.3    Lillo, M.P.4
  • 48
    • 33846287399 scopus 로고    scopus 로고
    • Structure and dynamics of proteins in crowded media: A time-resolved fluorescence polarization study
    • Kamp RM, Calvete J, Choli-Papadopoulou T (eds). Springer: Berlin
    • Zorrilla S, Rivas G, Lillo MP. 2004b. Structure and dynamics of proteins in crowded media: a time-resolved fluorescence polarization study. In Methods in Proteome and Protein Analysis (MPSA2002), Kamp RM, Calvete J, Choli-Papadopoulou T (eds). Springer: Berlin; 35-48.
    • (2004) Methods in Proteome and Protein Analysis (MPSA2002) , pp. 35-48
    • Zorrilla, S.1    Rivas, G.2    Lillo, M.P.3
  • 49
    • 1642285049 scopus 로고    scopus 로고
    • Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: Theory and application to concentrated solutions of ribonuclease
    • Zorrilla S, Jiménez M, Lillo MP, Rivas G, Minton AP. 2004c. Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease. Biophys. Chem. 108: 89-100.
    • (2004) Biophys. Chem. , vol.108 , pp. 89-100
    • Zorrilla, S.1    Jiménez, M.2    Lillo, M.P.3    Rivas, G.4    Minton, A.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.