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Volumn 83, Issue 8, 2012, Pages

An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for double kinetics experiments: Application to fluorescence resonance excitation energy transfer study of protein folding

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL TRANSITIONS; DATA COLLECTION; DECAY CURVES; DISTANCE DISTRIBUTIONS; EXCITATION PULSE; FAST ACQUISITION; FLUORESCENCE DECAYS; FLUORESCENCE RESONANCE; KINETIC EXPERIMENT; KINETICS EXPERIMENTS; KINETICS METHOD; LOW-NOISE DETECTION; MULTI-PHOTON PULSE; MULTIPARAMETERS; PICOSECOND RESOLUTION; PICOSECONDS; PULSE RECORDING; STOCHASTIC NOISE; SUB-MICROSECOND; TIME INTERVAL; TIME POINTS; TIME REGIME; TIME RESOLUTION; TIME-CORRELATED SINGLE PHOTON COUNTING; TIME-RESOLVED; WIDE SPECTRAL RANGE;

EID: 84865756639     PISSN: 00346748     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.4737632     Document Type: Review
Times cited : (17)

References (31)
  • 1
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • DOI 10.1016/S0968-0004(98)01345-0, PII S0968000498013450
    • R. L. Baldwin and G. D. Rose, Trends Biochem. Sci. 24 (2), 77 (1999); 10.1016/S0968-0004(98)01345-0 (Pubitemid 29346578)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.2 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 2
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • DOI 10.1016/S0968-0004(98)01346-2, PII S0968000498013462
    • R. L. Baldwin and G. D. Rose, Trends Biochem. Sci. 24 (1), 26 (1999); 10.1016/S0968-0004(98)01346-2 (Pubitemid 29074460)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 3
    • 0029858841 scopus 로고    scopus 로고
    • Observation of distinct nanosecond and microsecond protein folding events
    • DOI 10.1038/nsb1196-923
    • R. M. Ballew, J. Sabelko, and M. Gruebele, Nat. Struct. Biol. 3 (11), 923 (1996); 10.1038/nsb1196-923 (Pubitemid 26398324)
    • (1996) Nature Structural Biology , vol.3 , Issue.11 , pp. 923-926
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 4
    • 0030817794 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics and structure of the I form of apomyoglobin
    • DOI 10.1021/bi970634r
    • R. Gilmanshin, S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer, Biochemistry 36 (48), 15006 (1997). 10.1021/bi970634r (Pubitemid 27524427)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 15006-15012
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 5
    • 24044490917 scopus 로고    scopus 로고
    • Fast collapse but slow formation of secondary structure elements in the refolding transition of E. coli adenylate kinase
    • DOI 10.1016/j.jmb.2005.06.074, PII S0022283605007576
    • V. Ratner, D. Amir, E. Kahana, and E. Haas, J. Mol. Biol. 352 (3), 683 (2005). 10.1016/j.jmb.2005.06.074 (Pubitemid 41225478)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.3 , pp. 683-699
    • Ratner, V.1    Amir, D.2    Kahana, E.3    Haas, E.4
  • 9
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • DOI 10.1038/36626
    • V. Munoz, P. A. Thompson, J. Hofrichter, and W. A. Eaton, Nature (London) 390 (6656), 196 (1997); 10.1038/36626 (Pubitemid 27507992)
    • (1997) Nature , vol.390 , Issue.6656 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 10
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix⇆coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model
    • DOI 10.1021/bi9704764
    • P. A. Thompson, W. A. Eaton, and J. Hofrichter, Biochemistry 36 (30), 9200 (1997); 10.1021/bi9704764 (Pubitemid 27329505)
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 15
    • 0000192202 scopus 로고    scopus 로고
    • 10.1063/1.1148914
    • V. Ratner and E. Haas, Rev. Sci. Instrum. 69 (5), 2147 (1998). 10.1063/1.1148914
    • (1998) Rev. Sci. Instrum. , vol.69 , Issue.5 , pp. 2147
    • Ratner, V.1    Haas, E.2
  • 19
    • 0024675910 scopus 로고
    • 10.1016/S0006-3495(89)82918-2
    • J. M. Beechem and E. Haas, Biophys. J. 55 (6), 1225 (1989). 10.1016/S0006-3495(89)82918-2
    • (1989) Biophys. J. , vol.55 , Issue.6 , pp. 1225
    • Beechem, J.M.1    Haas, E.2
  • 20
    • 84981779372 scopus 로고
    • 10.1002/and19484370105
    • T. Förster, Ann. Phys. 437 (1-2), 55 (1948). 10.1002/andp. 19484370105
    • (1948) Ann. Phys. , vol.437 , Issue.12 , pp. 55
    • Förster, T.1
  • 21
    • 18744389451 scopus 로고    scopus 로고
    • The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements
    • DOI 10.1002/cphc.200400617
    • E. Haas, ChemPhysChem 6 (5), 858 (2005). 10.1002/cphc.200400617 (Pubitemid 40669549)
    • (2005) ChemPhysChem , vol.6 , Issue.5 , pp. 858-870
    • Haas, E.1
  • 22
    • 0026992556 scopus 로고
    • Nonlocal interactions stabilize compact folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitor
    • DOI 10.1021/bi00164a009
    • D. S. Gottfried and E. Haas, Biochemistry 31 (49), 12353 (1992); 10.1021/bi00164a009 (Pubitemid 23163110)
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12353-12362
    • Gottfried, D.S.1    Haas, E.2
  • 23
    • 0028936789 scopus 로고
    • 10.1021/bi00013a042
    • V. Ittah and E. Haas, Biochemistry 34 (13), 4493 (1995); 10.1021/bi00013a042
    • (1995) Biochemistry , vol.34 , Issue.13 , pp. 4493
    • Ittah, V.1    Haas, E.2
  • 24
    • 0034705335 scopus 로고    scopus 로고
    • 10.1006/jmbi.2000.3814
    • V. Ratner, M. Sinev, and E. Haas, J. Mol. Biol. 299 (5), 1363 (2000). 10.1006/jmbi.2000.3814
    • (2000) J. Mol. Biol. , vol.299 , Issue.5 , pp. 1363
    • Ratner, V.1    Sinev, M.2    Haas, E.3
  • 25
    • 0036071848 scopus 로고    scopus 로고
    • The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition
    • DOI 10.1016/S0022-2836(02)00520-X
    • V. Ratner, E. Kahana, and E. Haas, J. Mol. Biol. 320 (5), 1135 (2002). 10.1016/S0022-2836(02)00520-X (Pubitemid 34808829)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.5 , pp. 1135-1145
    • Ratner, V.1    Kahana, E.2    Haas, E.3
  • 27
    • 0017076991 scopus 로고
    • 10.1016/0003-2697(76)90077-4
    • A. Grinvald, Anal. Biochem. 75 (1), 260 (1976). 10.1016/0003-2697(76) 90077-4
    • (1976) Anal. Biochem. , vol.75 , Issue.1 , pp. 260
    • Grinvald, A.1
  • 28


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