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Volumn 84, Issue 1, 2003, Pages 599-611

Constrained analysis of fluorescence anisotropy decay: Application to experimental protein dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; PARVALBUMIN; TRYPTOPHAN;

EID: 12244255727     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74880-2     Document Type: Article
Times cited : (27)

References (38)
  • 1
    • 0018407386 scopus 로고
    • Time-resolved fluorescence measurements
    • Badea, M., and L. Brand. 1979. Time-resolved fluorescence measurements Methods Enzymol. 61:378-425.
    • (1979) Methods Enzymol. , vol.61 , pp. 378-425
    • Badea, M.1    Brand, L.2
  • 2
    • 0001163897 scopus 로고
    • Global resolution of heterogeneous decay by phase/modulation fluorometry: Mixtures and proteins
    • Beechem, J. M., J. R. Knutson, J. B. A. Ross, B. W. Turner, and L. Brand. 1983. Global resolution of heterogeneous decay by phase/modulation fluorometry: Mixtures and proteins. Biochemistry. 22:6054-6058.
    • (1983) Biochemistry , vol.22 , pp. 6054-6058
    • Beechem, J.M.1    Knutson, J.R.2    Ross, J.B.A.3    Turner, B.W.4    Brand, L.5
  • 4
    • 0031723406 scopus 로고    scopus 로고
    • Dynamics of biomolecules: Assignment of local motions by fluorescence anisotropy decay
    • Bialik, C. N., B. Wolf, E. L. Rachofsky, J. B. A. Ross, and W. R. Laws. 1998. Dynamics of biomolecules: Assignment of local motions by fluorescence anisotropy decay. Biophys. J. 75:2564-2573.
    • (1998) Biophys. J. , vol.75 , pp. 2564-2573
    • Bialik, C.N.1    Wolf, B.2    Rachofsky, E.L.3    Ross, J.B.A.4    Laws, W.R.5
  • 6
    • 0017106705 scopus 로고
    • Parvalbumins of white muscle of gadidae. 1. Extraction and purification of the parvalbumins of the whiting (Gadus merlangus L.), of the coalfish (G. virens L.), and of the haddock (G. aeglefinus L.)
    • Closset, J. I. 1976. Parvalbumins of white muscle of gadidae. 1. Extraction and purification of the parvalbumins of the whiting (Gadus merlangus L.), of the coalfish (G. virens L.), and of the haddock (G. aeglefinus L.). Comp. Biochem. Physiol. B. 55:531-535.
    • (1976) Comp. Biochem. Physiol. B , vol.55 , pp. 531-535
    • Closset, J.I.1
  • 7
    • 0021454425 scopus 로고
    • Analysis of time-resolved fluorescence anisotropy decays
    • Cross, A. J., and G. R. Fleming. 1984. Analysis of time-resolved fluorescence anisotropy decays. Biophys. J. 46:45-56.
    • (1984) Biophys. J. , vol.46 , pp. 45-56
    • Cross, A.J.1    Fleming, G.R.2
  • 8
    • 0001213596 scopus 로고
    • Membrane structure and dynamics by fluorescence probe depolarization kinetics
    • R.B. Cundall and R.E. Dale, editors. Plenum Press, New York
    • Dale, R. E. 1983. Membrane structure and dynamics by fluorescence probe depolarization kinetics. In Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology, R.B. Cundall and R.E. Dale, editors. Plenum Press, New York. 555-604.
    • (1983) Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology , pp. 555-604
    • Dale, R.E.1
  • 9
    • 0032881610 scopus 로고    scopus 로고
    • Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 Å) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core
    • Declerc, G. P., C. Evrard, V. Lamzin, and J. Parello. 1999. Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 Å) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core. Protein Sci. 8:2194-2204.
    • (1999) Protein Sci. , vol.8 , pp. 2194-2204
    • Declerc, G.P.1    Evrard, C.2    Lamzin, V.3    Parello, J.4
  • 10
    • 0024965968 scopus 로고
    • Fluorescence lifetime and solute quenching studies with the single tryptophan containing protein parvalbumin from codfish
    • Eftink, M. R., and Z. Wasylewski. 1989. Fluorescence lifetime and solute quenching studies with the single tryptophan containing protein parvalbumin from codfish. Biochemistry. 28:382-391.
    • (1989) Biochemistry , vol.28 , pp. 382-391
    • Eftink, M.R.1    Wasylewski, Z.2
  • 12
    • 85031258532 scopus 로고    scopus 로고
    • Local and rotational dynamics of calcium-binding proteins: New analysis methods for time-resolved fluorescence anisotropy
    • Abstr.
    • Feinstein, E., E. Rusinova, G. Deikus, E. L. Rachofsky, J. B. A. Ross, and W. R. Laws. 2001. Local and rotational dynamics of calcium-binding proteins: New analysis methods for time-resolved fluorescence anisotropy. Biophys. J. 80:361a. (Abstr.)
    • (2001) Biophys. J. , vol.80
    • Feinstein, E.1    Rusinova, E.2    Deikus, G.3    Rachofsky, E.L.4    Ross, J.B.A.5    Laws, W.R.6
  • 13
    • 0016075864 scopus 로고
    • On the analysis of fluorescence decay kinetics by the method of least squares
    • Grinvald, A., and I. Z. Steinberg. 1974. On the analysis of fluorescence decay kinetics by the method of least squares. Anal. Biochem. 59:583-598.
    • (1974) Anal. Biochem. , vol.59 , pp. 583-598
    • Grinvald, A.1    Steinberg, I.Z.2
  • 14
    • 0025339370 scopus 로고
    • Tryptophan-47 rotational isomerization in variant-3 scorpion neurotoxin. A combination thermodynamic perturbation and umbrella sampling study
    • Haydock, C., J. C. Sharp, and F. G. Prendergast. 1990. Tryptophan-47 rotational isomerization in variant-3 scorpion neurotoxin. A combination thermodynamic perturbation and umbrella sampling study. Biophys. J. 57:1269-1279.
    • (1990) Biophys. J. , vol.57 , pp. 1269-1279
    • Haydock, C.1    Sharp, J.C.2    Prendergast, F.G.3
  • 15
    • 0025295170 scopus 로고
    • A calcium specific conformational response of parvalbumin
    • Hutnik, C. M. L., J. P. MacManus, and A. G. Szabo. 1990. A calcium specific conformational response of parvalbumin. Biochemistry. 29:7318-7328.
    • (1990) Biochemistry , vol.29 , pp. 7318-7328
    • Hutnik, C.M.L.1    MacManus, J.P.2    Szabo, A.G.3
  • 16
    • 0028678827 scopus 로고
    • Calcium-binding proteins. 1: EF-hands
    • Kawasaki, H., and R. H. Kretsinger. 1994. Calcium-binding proteins. 1: EF-hands. Protein Profile. 1:343-517.
    • (1994) Protein Profile , vol.1 , pp. 343-517
    • Kawasaki, H.1    Kretsinger, R.H.2
  • 17
    • 0027303079 scopus 로고
    • Time-resolved fluorescence of the single tryptophan of bacillus stearothermophilus phosphofructokinase
    • Kim, S. J., F. N. Chowdhury, W. Styjewski, E. S. Younathan, P. S. Russo, and M. D. Barkley. 1993. Time-resolved fluorescence of the single tryptophan of bacillus stearothermophilus phosphofructokinase. Biophys. J. 65:215-226.
    • (1993) Biophys. J. , vol.65 , pp. 215-226
    • Kim, S.J.1    Chowdhury, F.N.2    Styjewski, W.3    Younathan, E.S.4    Russo, P.S.5    Barkley, M.D.6
  • 18
    • 0000060559 scopus 로고
    • Simultaneous analysis of multiple fluorescence decay curves: A global approach
    • Knutson, J. R., J. M. Beechem, and L. Brand. 1983. Simultaneous analysis of multiple fluorescence decay curves: A global approach. Chem. Phys. Lett. 102:501-507.
    • (1983) Chem. Phys. Lett. , vol.102 , pp. 501-507
    • Knutson, J.R.1    Beechem, J.M.2    Brand, L.3
  • 19
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger, R. H. 1980. Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8:119-174.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 20
    • 0015919772 scopus 로고
    • Carp muscle calcium binding protein. II. Structural determination and general description
    • Kretsinger, R. H., and C. E. Nockolds. 1973. Carp muscle calcium binding protein. II. Structural determination and general description. J. Biol. Chem. 248:3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 21
    • 0030973268 scopus 로고    scopus 로고
    • Conformational effects on calcium release from parvalbumin: Comparison of computational simulations with spectroscopic investigations
    • Laberge, M., W. W. Wright, K. Sudhakar, P. A. Liebman, and J. M. Vanderkooi. 1997. Conformational effects on calcium release from parvalbumin: Comparison of computational simulations with spectroscopic investigations. Biochemistry. 36:5363-5371.
    • (1997) Biochemistry , vol.36 , pp. 5363-5371
    • Laberge, M.1    Wright, W.W.2    Sudhakar, K.3    Liebman, P.A.4    Vanderkooi, J.M.5
  • 22
    • 42149099792 scopus 로고    scopus 로고
    • Kluwer Academic/Plenum Publishing, New York
    • nd Ed. Kluwer Academic/Plenum Publishing, New York.
    • (1999) nd Ed.
    • Lakowicz, J.R.1
  • 23
    • 0027976416 scopus 로고
    • Refined structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 Å resolution
    • McPhalen, C. A., A. R. Sielecki, B. D. Santarsiero, and M. N. James. 1994. Refined structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 Å resolution. J. Mol. Biol. 235:718-732.
    • (1994) J. Mol. Biol. , vol.235 , pp. 718-732
    • McPhalen, C.A.1    Sielecki, A.R.2    Santarsiero, B.D.3    James, M.N.4
  • 26
    • 0023376854 scopus 로고
    • Kinetics of dissociation of parvalbumin complexes with calcium and magnesium ions
    • Permiakov, E. A., A. V. Ostroyskii, L. P. Kalinichenko, and G. I. Deikus. 1987. Kinetics of dissociation of parvalbumin complexes with calcium and magnesium ions. Mol. Biol. 21:1017-1022.
    • (1987) Mol. Biol. , vol.21 , pp. 1017-1022
    • Permiakov, E.A.1    Ostroyskii, A.V.2    Kalinichenko, L.P.3    Deikus, G.I.4
  • 27
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • Petrich, J. W., M. C. Chang, D. B. McDonald, and G. R. Fleming. 1983. On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105:3824-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 28
    • 0033945095 scopus 로고    scopus 로고
    • Kinetic models and data analysis methods for fluorescence anisotropy decay
    • Rachofsky, E. L., and W. R. Laws. 2000. Kinetic models and data analysis methods for fluorescence anisotropy decay. Methods Enzymol. 321:216-238.
    • (2000) Methods Enzymol. , vol.321 , pp. 216-238
    • Rachofsky, E.L.1    Laws, W.R.2
  • 29
    • 0000476852 scopus 로고    scopus 로고
    • A general method for constrained analysis of fluorescence anisotropy decay: Application of the steady-state anisotropy
    • Rachofsky, E. L., B. Wolf, C. N. Bialik, J. B. A. Ross, and W. R. Laws. 1999. A general method for constrained analysis of fluorescence anisotropy decay: Application of the steady-state anisotropy. J. Fluorescence. 9:379-390.
    • (1999) J. Fluorescence , vol.9 , pp. 379-390
    • Rachofsky, E.L.1    Wolf, B.2    Bialik, C.N.3    Ross, J.B.A.4    Laws, W.R.5
  • 31
    • 85024692041 scopus 로고
    • Glycerol viscosity tables
    • Sheely, M. L. 1932. Glycerol viscosity tables. Ind. Eng. Chem. 24:1060-1064.
    • (1932) Ind. Eng. Chem. , vol.24 , pp. 1060-1064
    • Sheely, M.L.1
  • 32
    • 0000970090 scopus 로고
    • Least-squares analysis of fluorescence data
    • J.R. Lakowicz, editor. Plenum Press, New York
    • Straume, M., S. G. Frasier-Cadoret, and M. L. Johnson. 1991. Least-squares analysis of fluorescence data. In Topics in Fluorescence Spectroscopy, Vol 2. J.R. Lakowicz, editor. Plenum Press, New York. 177-240.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 177-240
    • Straume, M.1    Frasier-Cadoret, S.G.2    Johnson, M.L.3
  • 33
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo, A. G., and D. M. Rayner. 1980. Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102:554-563.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 34
    • 0016379969 scopus 로고
    • Fluorescent probe analysis of the lipid architecture of natural and experimental cholesterol-rich membranes
    • Vanderkooi, J., S. Fischkoff, B. Chance, and R. A. Cooper. 1974. Fluorescent probe analysis of the lipid architecture of natural and experimental cholesterol-rich membranes. Biochemistry. 13:1589-1595.
    • (1974) Biochemistry , vol.13 , pp. 1589-1595
    • Vanderkooi, J.1    Fischkoff, S.2    Chance, B.3    Cooper, R.A.4
  • 35
    • 0003157931 scopus 로고
    • Analysis of fluorescence anisotropy decays by a least squares method
    • Wahl, Ph. 1979. Analysis of fluorescence anisotropy decays by a least squares method. Biophys. Chem. 10:91-104.
    • (1979) Biophys. Chem. , vol.10 , pp. 91-104
    • Wahl, Ph.1
  • 36
    • 0027419731 scopus 로고
    • Human factor VIIa and its complex with soluble tissue factor: Evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods
    • Waxman, E., W. R. Laws, T. M. Laue, Y. Nemerson, and J. B. A. Ross. 1993. Human factor VIIa and its complex with soluble tissue factor: Evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods. Biochemistry. 32:3005-3012.
    • (1993) Biochemistry , vol.32 , pp. 3005-3012
    • Waxman, E.1    Laws, W.R.2    Laue, T.M.3    Nemerson, Y.4    Ross, J.B.A.5
  • 37
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer, D. B. 1962. Ultraviolet spectra of proteins and amino acids. Adv. Prot. Chem. 17:303-390.
    • (1962) Adv. Prot. Chem. , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 38
    • 0026701231 scopus 로고
    • Conformation of parathyroid hormone: Time-resolved fluorescence studies
    • Willis, K. J., and A. G. Szabo. 1992. Conformation of parathyroid hormone: Time-resolved fluorescence studies. Biochemistry. 31:8924-8931.
    • (1992) Biochemistry , vol.31 , pp. 8924-8931
    • Willis, K.J.1    Szabo, A.G.2


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