메뉴 건너뛰기




Volumn 54, Issue 1, 2000, Pages 1-15

Submicrosecond real-time fluorescence sampling: Application to protein folding

Author keywords

Apomyoglobin; Nonexponential kinetics; Phosphoglycerate kinase; Tryptophan; Ubiquitin

Indexed keywords

APOMYOGLOBIN; PHOSPHOGLYCERATE KINASE; TRYPTOPHAN; UBIQUITIN;

EID: 0033996482     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(00)00002-6     Document Type: Review
Times cited : (50)

References (51)
  • 1
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen S.J., Hofrichter J., Szabo A., Eaton W.A. Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA. 93:1996;11615-11617.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 2
    • 0033578370 scopus 로고    scopus 로고
    • The speed limit of protein folding measure by triplet-triplet energy transfer
    • Bieri O., Wirz J., Hellrung B., Schutkowski M., Drewello M., Kiefhaber T. The speed limit of protein folding measure by triplet-triplet energy transfer. PNAS. 96:1999;9597-9601.
    • (1999) PNAS , vol.96 , pp. 9597-9601
    • Bieri, O.1    Wirz, J.2    Hellrung, B.3    Schutkowski, M.4    Drewello, M.5    Kiefhaber, T.6
  • 3
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow M., Oliveberg M. High-energy channeling in protein folding. Biochemistry. 36:1997;7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 5
    • 0028960492 scopus 로고
    • How valid are denaturation-induced free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao M., Bolen D.W. How valid are denaturation-induced free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry. 34:1995;3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 7
    • 0001022344 scopus 로고    scopus 로고
    • The fast protein folding problem
    • Gruebele M. The fast protein folding problem. Annu. Rev. Phys. Chem. 50:1999;485-516.
    • (1999) Annu. Rev. Phys. Chem. , vol.50 , pp. 485-516
    • Gruebele, M.1
  • 10
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry. 29:1990;7134-7155.
    • (1990) Biochemistry , vol.29 , pp. 7134-7155
    • Dill, K.A.1
  • 11
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Afinsen C.B. Principles that govern the folding of protein chains. Science. 118:1973;223-230.
    • (1973) Science , vol.118 , pp. 223-230
    • Afinsen, C.B.1
  • 12
    • 0014633510 scopus 로고
    • The interaction of the ground and excited states of indole derivatives with electron scavengers
    • Steiner R.F., Kirby E.P. The interaction of the ground and excited states of indole derivatives with electron scavengers. J. Phys. Chem. 73:1969;4130-4135.
    • (1969) J. Phys. Chem. , vol.73 , pp. 4130-4135
    • Steiner, R.F.1    Kirby, E.P.2
  • 13
    • 0014940780 scopus 로고
    • The tryptophan microenvironments in apomyoglobin
    • Kirby E.P., Steiner R.F. The tryptophan microenvironments in apomyoglobin. J. Biol. Chem. 245:1970;6300-6306.
    • (1970) J. Biol. Chem. , vol.245 , pp. 6300-6306
    • Kirby, E.P.1    Steiner, R.F.2
  • 14
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluorezcenz
    • Förster T. Zwischenmolekulare Energiewanderung und Fluorezcenz. Ann. der Physik. 2:1948;55-75.
    • (1948) Ann. der Physik , vol.2 , pp. 55-75
    • Förster, T.1
  • 15
    • 0017027586 scopus 로고
    • Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group
    • Tsong T. Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group. Biochemistry. 15:1976;5467-5473.
    • (1976) Biochemistry , vol.15 , pp. 5467-5473
    • Tsong, T.1
  • 16
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz J.R., Weber G. Quenching of protein fluorescence by oxygen. detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry. 12:1973;4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 18
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Ann. Rev. Biochem. 47:1978;819-846.
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 19
    • 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., Mas M.T. 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. 36:1997;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
  • 20
    • 0029918121 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies of the molten globule state of apomyoglobin
    • Rischel C., Thyberg P., Rigler R., Poulsen F.M. Time-resolved fluorescence studies of the molten globule state of apomyoglobin. J. Mol. Biol. 257:1996;877-885.
    • (1996) J. Mol. Biol. , vol.257 , pp. 877-885
    • Rischel, C.1    Thyberg, P.2    Rigler, R.3    Poulsen, F.M.4
  • 21
  • 22
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem J.M., Brand L Time-resolved fluorescence of proteins. Ann. Rev. Biochem. 54:1985;43-71.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 23
    • 0017106725 scopus 로고
    • The fluorescence decay of tryptophan residues in native and denatured proteins
    • Grinvald A., Steinberg I.Z. The fluorescence decay of tryptophan residues in native and denatured proteins. Biochim. Biophys. Acta. 427:1976;663-678.
    • (1976) Biochim. Biophys. Acta , vol.427 , pp. 663-678
    • Grinvald, A.1    Steinberg, I.Z.2
  • 26
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry M.C.R., Roder H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat. Struct. Biol. 5:1998;385-392.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 27
    • 0015520134 scopus 로고
    • Dimerization of proflavin by the laser Raman temperature-jump method
    • Turner D.H., Flynn G.W., Lundberg S.K., Faller L.D., Sutin N. Dimerization of proflavin by the laser Raman temperature-jump method. Nature. 239:1972;215-217.
    • (1972) Nature , vol.239 , pp. 215-217
    • Turner, D.H.1    Flynn, G.W.2    Lundberg, S.K.3    Faller, L.D.4    Sutin, N.5
  • 29
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix↔coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model
    • Thompson P.A., Eaton W.A., Hofrichter J. Laser temperature jump study of the helix↔coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Biochemistry. 36:1997;9200-9210.
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 31
    • 0019885903 scopus 로고
    • Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase
    • Ross J.B.A., Schmidt C.J., Brand L. Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry. 20:1981;4369-4377.
    • (1981) Biochemistry , vol.20 , pp. 4369-4377
    • Ross, J.B.A.1    Schmidt, C.J.2    Brand, L.3
  • 32
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • Petrich J.W., Chang M.C., McDonald D.B., Fleming G.R. On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105:1983;3815-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3815-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 33
    • 0021101610 scopus 로고
    • Rotational freedom of tryptophan residues in proteins and peptides
    • Lakowicz J.R., Maliwai B.P., Cherek H., Balter A. Rotational freedom of tryptophan residues in proteins and peptides. Biochemistry. 22:1983;1742-1752.
    • (1983) Biochemistry , vol.22 , pp. 1742-1752
    • Lakowicz, J.R.1    Maliwai, B.P.2    Cherek, H.3    Balter, A.4
  • 34
    • 0001598267 scopus 로고
    • Quenching interactions and nonexponential decay: Tryptophan 138 of bacteriophage T4 lysozyme
    • Gilst M.V., Tang C., Roth A., Hudson B. Quenching interactions and nonexponential decay: tryptophan 138 of bacteriophage T4 lysozyme. J. Fluor. 4:1994;203-207.
    • (1994) J. Fluor. , vol.4 , pp. 203-207
    • Gilst, M.V.1    Tang, C.2    Roth, A.3    Hudson, B.4
  • 35
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • Teale F.W.J., Weber G. Ultraviolet fluorescence of the aromatic amino acids. Biochem. J. 65:1957;476-482.
    • (1957) Biochem. J. , vol.65 , pp. 476-482
    • Teale, F.W.J.1    Weber, G.2
  • 36
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elöve G., Chaffotte A., Roder H., Goldberg M. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry. 31:1992;6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.1    Chaffotte, A.2    Roder, H.3    Goldberg, M.4
  • 37
    • 0028892701 scopus 로고
    • Modification of a specific tyrosine enables tracing of the end-to-end distance during apomyoglobin folding
    • Rischel C., Poulsen F.M. Modification of a specific tyrosine enables tracing of the end-to-end distance during apomyoglobin folding. FEBS Lett. 374:1995;105-109.
    • (1995) FEBS Lett. , vol.374 , pp. 105-109
    • Rischel, C.1    Poulsen, F.M.2
  • 38
    • 0031095826 scopus 로고    scopus 로고
    • Rate of intrachain diffusion of unfolded cytochrome c
    • Hagen S.J., Hofrichter J., Eaton W.A. Rate of intrachain diffusion of unfolded cytochrome c. J. Phys. Chem. B. 101:1997;2352-2365.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 2352-2365
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 39
    • 0030916895 scopus 로고    scopus 로고
    • Picosecond fluorescence decay curves collected on millisecond time scale: Direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions
    • Beechem J.M. Picosecond fluorescence decay curves collected on millisecond time scale: direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions. Methods Enzymol. 278:1997;24-49.
    • (1997) Methods Enzymol. , vol.278 , pp. 24-49
    • Beechem, J.M.1
  • 40
    • 0033616632 scopus 로고    scopus 로고
    • Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time
    • Bilsel O., Yang L., Zitzewitz J.A., Beechem J.M., Mathews C.R. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry. 38:1999;4177-4187.
    • (1999) Biochemistry , vol.38 , pp. 4177-4187
    • Bilsel, O.1    Yang, L.2    Zitzewitz, J.A.3    Beechem, J.M.4    Mathews, C.R.5
  • 42
    • 0000864144 scopus 로고    scopus 로고
    • The cold denatured ensemble of apomyoglobin: Implications for the early steps of folding
    • Sabelko J., Ervin J., Gruebele M. The cold denatured ensemble of apomyoglobin: implications for the early steps of folding. J. Phys. Chem. B. 102:1998;1806-1819.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 1806-1819
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 44
    • 36849104119 scopus 로고
    • Laser temperature-jump apparatus for relaxation studies in electrolytic solutions
    • Hoffmann H., Yeager E., Stuehr J. Laser temperature-jump apparatus for relaxation studies in electrolytic solutions. Rev. Sci. Instrum. 39:1968;649-653.
    • (1968) Rev. Sci. Instrum. , vol.39 , pp. 649-653
    • Hoffmann, H.1    Yeager, E.2    Stuehr, J.3
  • 45
    • 0001288529 scopus 로고
    • Nanosecond temperature-jump technique with an iodine laser
    • Holzwarth J.F., Schmidt A., Wolff H., Volk R. Nanosecond temperature-jump technique with an iodine laser. J. Phys. Chem. 81:1977;2300-2301.
    • (1977) J. Phys. Chem. , vol.81 , pp. 2300-2301
    • Holzwarth, J.F.1    Schmidt, A.2    Wolff, H.3    Volk, R.4
  • 47
    • 0001261542 scopus 로고    scopus 로고
    • A single-sweep, nanosecond time resolution laser temperature-jump apparatus
    • Ballew R.M., Sabelko J., Reiner C., Gruebele M. A single-sweep, nanosecond time resolution laser temperature-jump apparatus. Rev. Sci. Instrum. 67:1996;3694-3699.
    • (1996) Rev. Sci. Instrum. , vol.67 , pp. 3694-3699
    • Ballew, R.M.1    Sabelko, J.2    Reiner, C.3    Gruebele, M.4
  • 48
    • 0029858841 scopus 로고    scopus 로고
    • Observation of distinct nanosecond and microsecond protein folding events
    • Ballew R.M., Sabelko J., Gruebele M. Observation of distinct nanosecond and microsecond protein folding events. Nat. Struct. Biol. 3:1996;923-926.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 923-926
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 49
    • 0141598688 scopus 로고    scopus 로고
    • Characterization of the 3-D structure and psec/nsec rotational dynamics of the rapidly collapsed folded state in yeast phosphoglycerate kinase
    • Tu-Pos-130
    • P. Lillo, M.T. Mas, J.M. Beechem, Characterization of the 3-D structure and psec/nsec rotational dynamics of the rapidly collapsed folded state in yeast phosphoglycerate kinase, Biophys. J. 74 (1998) Tu-Pos-130.
    • (1998) Biophys. J. , vol.74
    • Lillo, P.1    Mas, M.T.2    Beechem, J.M.3
  • 50
  • 51
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry E.R., Hofrichter J. Singular value decomposition: application to analysis of experimental data. Methods Enzymol. 210:1992;129-192.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.