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Volumn 11, Issue 3, 2000, Pages 352-362

Design consideration and probes for fluorescence resonance energy transfer studies

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENERGY TRANSFER; ESCHERICHIA COLI; PROBES; PROTEINS;

EID: 0034117516     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc990132l     Document Type: Article
Times cited : (27)

References (35)
  • 1
    • 0024675910 scopus 로고
    • Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements
    • Beechem, J. M., and Haas, E. (1989) Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements. Biophys. J. 55, 1225-1236.
    • (1989) Biophys. J. , vol.55 , pp. 1225-1236
    • Beechem, J.M.1    Haas, E.2
  • 3
    • 0025747957 scopus 로고
    • Synthesis and fluorescent properties of some heterobifunctional and rigidized 7-aminocoumarins
    • Besson, T., Coudert, G., and Guillaumet, G. (1991) Synthesis and fluorescent properties of some heterobifunctional and rigidized 7-aminocoumarins. J. Heterocycl. Chem. 28, 1517-1523.
    • (1991) J. Heterocycl. Chem. , vol.28 , pp. 1517-1523
    • Besson, T.1    Coudert, G.2    Guillaumet, G.3
  • 4
    • 0022423609 scopus 로고
    • Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli
    • Brune, M., Schumann, R., and Wittinghofer, A. (1985) Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 13, 7139-7151.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 7139-7151
    • Brune, M.1    Schumann, R.2    Wittinghofer, A.3
  • 5
    • 0033105255 scopus 로고    scopus 로고
    • Thiol-reactive luminescent chelates of terbium and europium
    • Chen, J., and Selvin, P. R. (1999) Thiol-reactive luminescent chelates of terbium and europium. Bioconjugate Chem. 10, 311-315.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 311-315
    • Chen, J.1    Selvin, P.R.2
  • 7
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale, R. E., Eisinger, J., and Blumberg, W. E. (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26, 161-194.
    • (1979) Biophys. J. , vol.26 , pp. 161-194
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 9
    • 0023100239 scopus 로고
    • Structural and catalytic characteristics of Escherichia coli adenylate kinase
    • Girons, I. S., Gilles, A.-M., Margarita, D., Michelson, S., Monot, M., Fermandjian, S., Biophys. J. 26, 161-194; Danchin, A., and B?rzu, O. (1987) Structural and catalytic characteristics of Escherichia coli adenylate kinase. J. Biol. Chem. 262, 622-629.
    • (1987) J. Biol. Chem. , vol.262 , pp. 622-629
    • Danchin, A.1    Brzu, O.2
  • 10
    • 0016075864 scopus 로고
    • On the analysis of fluorescence decay kinetics by the method of least-squares
    • Grinvald, A., and Steinberg, I. Z. (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
  • 11
    • 0030348362 scopus 로고    scopus 로고
    • The problem of protein folding and dynamics: Time-resolved dynamic nonradiative excitation energy transfer measurements
    • Haas, E. (1996) The problem of protein folding and dynamics: time-resolved dynamic nonradiative excitation energy transfer measurements. IEEE J. Sel. Top. Quantum Electron. 2, 1088-1106.
    • (1996) IEEE J. Sel. Top. Quantum Electron. , vol.2 , pp. 1088-1106
    • Haas, E.1
  • 12
    • 0027074883 scopus 로고
    • Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer
    • Haran, G., Haas, E., Szpikowska, B. K., and Mas, M. T. (1992) Domain motions in phosphoglycerate kinase: determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer. Proc. Natl. Acad. Sci. U.S.A. 89, 11764-11768.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11764-11768
    • Haran, G.1    Haas, E.2    Szpikowska, B.K.3    Mas, M.T.4
  • 13
    • 0021508431 scopus 로고
    • Intramolecular dynamics of chain molecules monitored by fluctuations in efficiency of excitation energy transfer
    • A Theoretical Study
    • Haas, E., and Steinberg, I. Z. (1984) Intramolecular Dynamics of Chain Molecules Monitored by Fluctuations in Efficiency of Excitation Energy Transfer. A Theoretical Study. Biophys. J. 46, 429-437.
    • (1984) Biophys. J. , vol.46 , pp. 429-437
    • Haas, E.1    Steinberg, I.Z.2
  • 15
    • 0021509340 scopus 로고
    • Multifunctional cross-linking reagents. I. Synthesis and properties of novel photoactivable, thiol-directed fluorescent reagents
    • Kanaoka, Y., Kobayashi, A., Sato, E., Nakayama, H., Ueno, T., Muno, D., and Sekine, T. (1984) Multifunctional cross-linking reagents. I. Synthesis and properties of novel photoactivable, thiol-directed fluorescent reagents. Chem. Pharm. Bull. 32, 3926-3933.
    • (1984) Chem. Pharm. Bull. , vol.32 , pp. 3926-3933
    • Kanaoka, Y.1    Kobayashi, A.2    Sato, E.3    Nakayama, H.4    Ueno, T.5    Muno, D.6    Sekine, T.7
  • 16
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 17
    • 0025760572 scopus 로고
    • Correction for incomplete labeling in the measurement of distance distributions by frequency-domain fluorometry
    • Lakowicz, J. R., Gryczynski, I., Wiczk, W., Kusba, J., and Johnson, M. L. (1991) Correction for incomplete labeling in the measurement of distance distributions by frequency-domain fluorometry. Anal. Biochem. 195, 243-254.
    • (1991) Anal. Biochem. , vol.195 , pp. 243-254
    • Lakowicz, J.R.1    Gryczynski, I.2    Wiczk, W.3    Kusba, J.4    Johnson, M.L.5
  • 18
    • 0030964626 scopus 로고    scopus 로고
    • Design and characterization of a multisite fluorescence energy-transfer system for protein folding studies: A steady-state and time-resolved study of yeast phosphoglycerate kinase
    • Lillo, M. P., Beechem, J. M., Szpikowska, B. K., Sherman, M. A., and Mas, M. T. (1997a) Design and characterization of a multisite fluorescence energy-transfer system for protein folding studies: a steady-state and time-resolved study of yeast phosphoglycerate kinase. Biochemistry 36, 11261-11272.
    • (1997) Biochemistry , vol.36 , pp. 11261-11272
    • Lillo, M.P.1    Beechem, J.M.2    Szpikowska, B.K.3    Sherman, M.A.4    Mas, M.T.5
  • 19
    • 0030964627 scopus 로고    scopus 로고
    • Real-time measurement of multiple intramolecular distances during protein folding reactions: A multisite stopped-flow fluorescence energy-transfer study of yeast phosphoglycerate kinase
    • Lillo, M. P., Szpikowska, B. K., Mas, M. T., Sutin, J. D., and Beechem, J. M. (1997b) Real-time measurement of multiple intramolecular distances during protein folding reactions: a multisite stopped-flow fluorescence energy-transfer study of yeast phosphoglycerate kinase. Biochemistry 36, 11273-11281.
    • (1997) Biochemistry , vol.36 , pp. 11273-11281
    • Lillo, M.P.1    Szpikowska, B.K.2    Mas, M.T.3    Sutin, J.D.4    Beechem, J.M.5
  • 21
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35, 7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 22
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • Müller, C. W., Schlauderer, G. J., Reinstein, J., and Schulz, G. E. (1996) Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure 4, 147-156.
    • (1996) Structure , vol.4 , pp. 147-156
    • Müller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 23
    • 0024298856 scopus 로고
    • Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli
    • Reinstein, J., Brune, M., and Wittinghofer, A. (1988) Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry 27, 4712-4720.
    • (1988) Biochemistry , vol.27 , pp. 4712-4720
    • Reinstein, J.1    Brune, M.2    Wittinghofer, A.3
  • 24
    • 0014429881 scopus 로고
    • Initial velocity and equilibrium kinetics of myokinase
    • Rhoads, D. G., and Lowenstein, J. M. (1968) Initial velocity and equilibrium kinetics of myokinase. J. Biol. Chem. 243, 3963-3972.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3963-3972
    • Rhoads, D.G.1    Lowenstein, J.M.2
  • 25
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-dithiobis (2-nitrobenzoic acid) - A reexamination
    • Riddles, P. W., Blakely, R. L., and Zerner, B. (1979) Ellman's reagent: 5,5′-dithiobis (2-nitrobenzoic acid) - a reexamination. Anal. Biochem. 94, 75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakely, R.L.2    Zerner, B.3
  • 26
    • 33947445404 scopus 로고
    • Preparation of 4-qinolinols by the ethyl ethoxalyl acetate method
    • Riegel, B., Albisetti, J. C., Jr., Lappin, G. R., and Baker, R. H. (1946) Preparation of 4-qinolinols by the ethyl ethoxalyl acetate method. J. Am. Chem. Soc. 68, 2685-2688.
    • (1946) J. Am. Chem. Soc. , vol.68 , pp. 2685-2688
    • Riegel, B.1    Albisetti J.C., Jr.2    Lappin, G.R.3    Baker, R.H.4
  • 27
    • 0028077111 scopus 로고
    • Luminescence energy transfer using a terbium chelate: Improvements on fluorescence energy transfer
    • Selvin, P. R., and Hearst, J. E. (1994) Luminescence energy transfer using a terbium chelate: improvements on fluorescence energy transfer. Proc. Natl. Acad. Sci. U.S.A. 91, 10024-10028.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10024-10028
    • Selvin, P.R.1    Hearst, J.E.2
  • 29
    • 0030592693 scopus 로고    scopus 로고
    • Towards a mechanism of AMP-substrate inhibition in adenylate kinase from Escherichia coli
    • Sinev, M. A., Sineva, E. V., Ittah, V., and Haas, E. (1996b) Towards a mechanism of AMP-substrate inhibition in adenylate kinase from Escherichia coli. FEBS Lett. 397, 273-276.
    • (1996) FEBS Lett. , vol.397 , pp. 273-276
    • Sinev, M.A.1    Sineva, E.V.2    Ittah, V.3    Haas, E.4
  • 30
    • 0028861599 scopus 로고
    • Metal-ligand complexes as a new class of long-lived fluorophores for protein hydrodynamics
    • Terpetschnig, E., Szmacinski, H., Malak, H., and Lakowicz, J. R. (1995) Metal-ligand complexes as a new class of long-lived fluorophores for protein hydrodynamics. Biophys. J. 68, 342-350.
    • (1995) Biophys. J. , vol.68 , pp. 342-350
    • Terpetschnig, E.1    Szmacinski, H.2    Malak, H.3    Lakowicz, J.R.4
  • 33
    • 0025398294 scopus 로고
    • A general method for highly selective cross-linking of unprotected polypeptides via pH-controlled modification of N-terminal á-amino groups
    • Wetzel, R., Halualani, R., Stults, J. T., and Quan, C. (1990) A general method for highly selective cross-linking of unprotected polypeptides via pH-controlled modification of N-terminal á-amino groups. Bioconjugate Chem. 1, 114-122.
    • (1990) Bioconjugate Chem. , vol.1 , pp. 114-122
    • Wetzel, R.1    Halualani, R.2    Stults, J.T.3    Quan, C.4
  • 34
    • 0017874456 scopus 로고
    • Cooligopeptides containing aromatic residues spaced by glycyl residues. IX. Fluorescence properties of tryptophan-containing peptides
    • Wiget, P., and Luisi, P. L. (1978) Cooligopeptides containing aromatic residues spaced by glycyl residues. IX. Fluorescence Properties of tryptophan-containing peptides. Biopolymers 17, 167-180.
    • (1978) Biopolymers , vol.17 , pp. 167-180
    • Wiget, P.1    Luisi, P.L.2
  • 35
    • 0026708349 scopus 로고
    • Novel cyclization chemistry especially suited for biologically derived, unprotected peptides
    • Wood, S. J., and Wetzel, R. (1992) Novel cyclization chemistry especially suited for biologically derived, unprotected peptides. Int. J. Pept. Protein Res. 39, 533-539.
    • (1992) Int. J. Pept. Protein Res. , vol.39 , pp. 533-539
    • Wood, S.J.1    Wetzel, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.