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Volumn 1, Issue , 2008, Pages 491-535

Early Events in Protein Folding Explored by Rapid Mixing Methods

Author keywords

Computer; Events; Proteins; Simulations; Techniques

Indexed keywords


EID: 84889765760     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch15     Document Type: Chapter
Times cited : (7)

References (146)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E. (1998). How do small single-domain proteins fold? Fold. Des. 3, R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 2
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews, C. R. (1987). Effect of point mutations on the folding of globular proteins. Meth. Enzymol. 154, 498-511.
    • (1987) Meth. Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 3
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek, A., Kellis, J. T., Jr., Serrano, L. & Fersht, A. R. (1989). Mapping the transition state and pathway of protein folding by protein engineering. Nature 340, 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 4
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of the chymotrypsin inhibitor-2: A critical test of the protein engineering method of analysis
    • Jackson, S. E., elMasry, N. & Fersht, A. R. (1993). Structure of the hydrophobic core in the transition state for folding of the chymotrypsin inhibitor-2: A critical test of the protein engineering method of analysis. Biochemistry 32, 11270-11278.
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    El Masry, N.2    Fersht, A.R.3
  • 5
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C. R. (1993). Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 6
    • 0028082357 scopus 로고
    • Probing the structure of folding intermediates
    • Evans, P. A. & Radford, S. E. (1994). Probing the structure of folding intermediates. Curr. Opin. Struct. Biol. 4, 100-106.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 100-106
    • Evans, P.A.1    Radford, S.E.2
  • 7
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Coló n, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 8
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin, R. L. & Rose, G. D. (1999). Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24, 77-83.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 9
    • 0037949453 scopus 로고    scopus 로고
    • Early stages of protein folding
    • In Mechanisms of protein folding (Pain, R. H., ed.), Oxford University Press, New York
    • Roder, H., Elöve, G. A. & Shastry, R. M. C. (2000). Early stages of protein folding. In Mechanisms of protein folding (Pain, R. H., ed.), pp. 65-104. Oxford University Press, New York.
    • (2000) , pp. 65-104
    • Roder, H.1    Elöve, G.A.2    Shastry, R.M.C.3
  • 11
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S. & Baldwin, R. L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 12
    • 0032844656 scopus 로고    scopus 로고
    • Methods for exploring early events in protein folding
    • Roder, H. & Shastry, M. C. R. (1999). Methods for exploring early events in protein folding. Curr. Opin. Struct. Biol. 9, 620-626.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 620-626
    • Roder, H.1    Shastry, M.C.R.2
  • 13
    • 0022965254 scopus 로고
    • Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons
    • Roder, H. & Wüthrich, K. (1986). Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons. Proteins 1, 34-42.
    • (1986) Proteins , vol.1 , pp. 34-42
    • Roder, H.1    Wüthrich, K.2
  • 14
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by Hexchange labelling and proton NMR
    • Roder, H., Elöve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by Hexchange labelling and proton NMR. Nature 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 15
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar, J. B. & Baldwin, R. L. (1988). NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature 335, 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 16
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D. & Wolynes, P. G. (1995). Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 17
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: bringing together theory and experiment
    • Dobson, C. M. & Karplus, M. (1999). The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9, 92-101.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 19
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • Jones, C. M., Henry, E. R., Hu, Y. et al. (1993). Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl Acad. Sci. USA 90, 11860-11864.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11860-11864
    • Jones, C.M.1    Henry, E.R.2    Hu, Y.3
  • 21
    • 0001022344 scopus 로고    scopus 로고
    • The fast protein folding problem
    • Gruebele, M. (1999). The fast protein folding problem. Annu. Rev. Phys. Chem. 50, 485-516.
    • (1999) Annu. Rev. Phys. Chem. , vol.50 , pp. 485-516
    • Gruebele, M.1
  • 26
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixer to monitor reactions on the microsecond time scale
    • Shastry, M. C. R., Luck, S. D. & Roder, H. (1998). A continuous-flow capillary mixer to monitor reactions on the microsecond time scale. Biophys. J. 74, 2714-2721.
    • (1998) Biophys. J. , vol.74 , pp. 2714-2721
    • Shastry, M.C.R.1    Luck, S.D.2    Roder, H.3
  • 27
    • 0033621117 scopus 로고    scopus 로고
    • Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering
    • Pollack, L., Tate, M. W., Darnton, N. C. et al. (1999). Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proc. Natl Acad. Sci. USA 96, 10115-10117.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10115-10117
    • Pollack, L.1    Tate, M.W.2    Darnton, N.C.3
  • 28
    • 0242503695 scopus 로고
    • The velocity with which carbon monoxide displaces oxygen from combination with heamoglobin
    • Hartridge, H. & Roughton, F. J. W. (1923). The velocity with which carbon monoxide displaces oxygen from combination with heamoglobin. I. Proc. R. Soc. (Lond.) B Biol. Sci. 94, 336-367.
    • (1923) I. Proc. R. Soc. (Lond.) B Biol. Sci. , vol.94 , pp. 336-367
    • Hartridge, H.1    Roughton, F.J.W.2
  • 29
    • 0000750623 scopus 로고
    • Biochem. J.
    • Gibson, Q. H. & Milnes, L. (1964). Biochem. J. 91, 161.
    • (1964) , vol.91 , pp. 161
    • Gibson, Q.H.1    Milnes, L.2
  • 30
    • 0004159907 scopus 로고
    • Rapid Mixing and Sampling Techniques in Biochemistry
    • (Chance, B., Eisenhardt, R. H., Gibson, Q. H. & Lonberg-Holm, K. K., Eds), Academic Press, New York
    • Chance, B. (1964). Rapid Mixing and Sampling Techniques in Biochemistry. (Chance, B., Eisenhardt, R. H., Gibson, Q. H. & Lonberg-Holm, K. K., Eds), Academic Press, New York.
    • (1964)
    • Chance, B.1
  • 33
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry, M. C. R. & Roder, H. (1998). Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Struct. Biol. 5, 385-392.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 34
    • 0542421561 scopus 로고    scopus 로고
    • Kinetic and structural analysis of submillisecond folding events in cytochrome c
    • Shastry, M. C. R., Sauder, J. M. & Roder, H. (1998). Kinetic and structural analysis of submillisecond folding events in cytochrome c. Acc. Chem. Res. 31, 717-725.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 717-725
    • Shastry, M.C.R.1    Sauder, J.M.2    Roder, H.3
  • 35
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
    • Park, S.-H., Shastry, M. C. R. & Roder, H. (1999). Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nature Struct. Biol. 6, 943-947.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 943-947
    • Park, S.-H.1    Shastry, M.C.R.2    Roder, H.3
  • 37
    • 0035150938 scopus 로고    scopus 로고
    • Structural and kinetic characterization of early folding events in beta-lactoglobulin
    • Kuwata, K., Shastry, R., Cheng, H. et al. (2001). Structural and kinetic characterization of early folding events in beta-lactoglobulin. Nature Struct. Biol. 8, 151-155.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 151-155
    • Kuwata, K.1    Shastry, R.2    Cheng, H.3
  • 38
    • 0037162450 scopus 로고    scopus 로고
    • Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
    • Teilum, K., Maki, K., Kragelund, B. B., Poulsen, F. M. & Roder, H. (2002). Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proc. Natl Acad. Sci. USA 99, 9807-9812.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9807-9812
    • Teilum, K.1    Maki, K.2    Kragelund, B.B.3    Poulsen, F.M.4    Roder, H.5
  • 41
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates
    • Johnson, K. A. (1995). Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates. Meth. Enzymol. 249, 38-61.
    • (1995) Meth. Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 42
    • 0000035628 scopus 로고    scopus 로고
    • Hydrodynamic focusing on a silicon chip: Mixing nanoliters in microseconds
    • Knight, J. B., Vishwanath, A., Brody, J. P. & Austin, R. H. (1998). Hydrodynamic focusing on a silicon chip: Mixing nanoliters in microseconds. Phys. Rev. Lett. 80, 3863-3866.
    • (1998) Phys. Rev. Lett. , vol.80 , pp. 3863-3866
    • Knight, J.B.1    Vishwanath, A.2    Brody, J.P.3    Austin, R.H.4
  • 43
    • 0036841867 scopus 로고    scopus 로고
    • Laminar-flow fluid mixer for fast fluorescence kinetics studies
    • Pabit, S. A. & Hagen, S. J. (2002). Laminar-flow fluid mixer for fast fluorescence kinetics studies. Biophys. J. 83, 2872-2878.
    • (2002) Biophys. J. , vol.83 , pp. 2872-2878
    • Pabit, S.A.1    Hagen, S.J.2
  • 44
    • 0023669402 scopus 로고
    • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
    • Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. & Nagamura, T. (1987). Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 221, 115-118.
    • (1987) FEBS Lett. , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 45
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elöve, G. A., Chaffotte, A. F., Roder, H. & Goldberg, M. E. (1992). Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry 31, 6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 46
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A. & Wright, P. E. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-895.
    • (1993) Science , vol.262 , pp. 892-895
    • Jennings, P.A.1    Wright, P.E.2
  • 47
    • 0028947956 scopus 로고
    • Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones, B. E. & Matthews, C. R. (1995). Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 4, 167-177.
    • (1995) Protein Sci. , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 48
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I. D. & Roder, H. (1996). Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3, 193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 49
    • 0036135965 scopus 로고    scopus 로고
    • Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange
    • Walkenhorst, W. F., Edwards, J. A., Markley, J. L. & Roder, H. (2002). Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange. Protein Sci 11, 82-91.
    • (2002) Protein Sci , vol.11 , pp. 82-91
    • Walkenhorst, W.F.1    Edwards, J.A.2    Markley, J.L.3    Roder, H.4
  • 50
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N-and Cterminal helices plays a critical role in the kinetics of cytochrome c folding
    • Coló n, W., Elöve, G. A., Wakem, L. P., Sherman, F. & Roder, H. (1996). Side chain packing of the N-and Cterminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry 35, 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 51
    • 0018450898 scopus 로고
    • Measurement of the dead time of a fluorescence stopped-flow instrument
    • Peterman, B. F. (1979). Measurement of the dead time of a fluorescence stopped-flow instrument. Anal. Biochem. 93, 442-444.
    • (1979) Anal. Biochem. , vol.93 , pp. 442-444
    • Peterman, B.F.1
  • 52
    • 0014278035 scopus 로고
    • High resolution mixer for the study of the kinetics of rapid reactions in solution
    • Berger, R. L. & Chapman, H. F. (1968). High resolution mixer for the study of the kinetics of rapid reactions in solution. Rev. Sci. Instrum. 39, 493-498.
    • (1968) Rev. Sci. Instrum. , vol.39 , pp. 493-498
    • Berger, R.L.1    Chapman, H.F.2
  • 54
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y. & Barkley, M. D. (1998). Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 55
    • 0001598267 scopus 로고
    • Quenching interactions and nonexponential decay: Tryptophan 138 of bacteriophage T4 lysozyme
    • Van Gilst, M., Tang, C., Roth, A. & Hudson, B. (1994). Quenching interactions and nonexponential decay: Tryptophan 138 of bacteriophage T4 lysozyme. Fluorescence 4, 203-207.
    • (1994) Fluorescence , vol.4 , pp. 203-207
    • Van Gilst, M.1    Tang, C.2    Roth, A.3    Hudson, B.4
  • 56
    • 0031784567 scopus 로고    scopus 로고
    • Probing the folding pathway of a beta-clam protein with single-tryptophan constructs
    • Clark, P. L., Weston, B. F. & Gierasch, L. M. (1998). Probing the folding pathway of a beta-clam protein with single-tryptophan constructs. Fold. Des. 3, 401-412.
    • (1998) Fold. Des. , vol.3 , pp. 401-412
    • Clark, P.L.1    Weston, B.F.2    Gierasch, L.M.3
  • 57
    • 0032568498 scopus 로고    scopus 로고
    • Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate
    • Shao, X. & Matthews, C. R. (1998). Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry 37, 7850-7858.
    • (1998) Biochemistry , vol.37 , pp. 7850-7858
    • Shao, X.1    Matthews, C.R.2
  • 58
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophancontaining mutant of ubiquitin
    • Khorasanizadeh, S., Peters, I. D., Butt, T. R. & Roder, H. (1993). Folding and stability of a tryptophancontaining mutant of ubiquitin. Biochemistry 32, 7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 59
    • 0030971246 scopus 로고    scopus 로고
    • Fluorescence methods for studying kinetics of protein-folding reactions
    • Eftink, M. R. & Shastry, M. C. R. (1997). Fluorescence methods for studying kinetics of protein-folding reactions. Meth. Enzymol. 278, 258-286.
    • (1997) Meth. Enzymol. , vol.278 , pp. 258-286
    • Eftink, M.R.1    Shastry, M.C.R.2
  • 60
    • 1842609473 scopus 로고    scopus 로고
    • Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing
    • Maki, K., Cheng, H., Dolgikh, D. A., Shastry, M. C. & Roder, H. (2004). Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. J. Mol. Biol. 338, 383-400.
    • (2004) J. Mol. Biol. , vol.338 , pp. 383-400
    • Maki, K.1    Cheng, H.2    Dolgikh, D.A.3    Shastry, M.C.4    Roder, H.5
  • 61
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer, L. (1968). Fluorescence spectroscopy of proteins. Science 162, 526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 63
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates
    • Engelhard, M. & Evans, P. A. (1995). Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci. 4, 1553-1562.
    • (1995) Protein Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 64
    • 0016380496 scopus 로고
    • The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation
    • Tsong, T. Y. (1974). The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation. J. Biol. Chem. 249, 1988-1990.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1988-1990
    • Tsong, T.Y.1
  • 65
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Coló n, W. & Roder, H. (1996). Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct. Biol. 3, 1019-1025.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1019-1025
    • Colón, W.1    Roder, H.2
  • 66
    • 0017845014 scopus 로고
    • Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by l-ascorbic acid
    • Tonomura, B., Nakatani, H., Ohnishi, M., Yamaguchi-Ito, J. & Hiromi, K. (1978). Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by l-ascorbic acid. Anal. Biochem. 84, 370-383.
    • (1978) Anal. Biochem. , vol.84 , pp. 370-383
    • Tonomura, B.1    Nakatani, H.2    Ohnishi, M.3    Yamaguchi-Ito, J.4    Hiromi, K.5
  • 68
    • 0842299585 scopus 로고    scopus 로고
    • Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of a-helical content and compactness
    • Uzawa, T., Akiyama, S., Kimura, T. et al. (2004). Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of a-helical content and compactness. Proc. Natl Acad. Sci. USA 101, 1171-1176.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1171-1176
    • Uzawa, T.1    Akiyama, S.2    Kimura, T.3
  • 69
    • 0034063443 scopus 로고    scopus 로고
    • Variable velocity liquid flow EPR applied to submillisecond protein folding
    • Grigoryants, V. M., Veselov, A. V. & Scholes, C. P. (2000). Variable velocity liquid flow EPR applied to submillisecond protein folding. Biophys. J. 78, 2702-2708.
    • (2000) Biophys. J. , vol.78 , pp. 2702-2708
    • Grigoryants, V.M.1    Veselov, A.V.2    Scholes, C.P.3
  • 70
    • 0035951095 scopus 로고    scopus 로고
    • EPR-detected folding kinetics of externally located cysteine-directed spin-labeled mutants of iso-1-cytochrome c
    • DeWeerd, K., Grigoryants, V., Sun, Y., Fetrow, J. S. & Scholes, C. P. (2001). EPR-detected folding kinetics of externally located cysteine-directed spin-labeled mutants of iso-1-cytochrome c. Biochemistry 40, 15846-15855.
    • (2001) Biochemistry , vol.40 , pp. 15846-15855
    • DeWeerd, K.1    Grigoryants, V.2    Sun, Y.3    Fetrow, J.S.4    Scholes, C.P.5
  • 71
    • 0035926229 scopus 로고    scopus 로고
    • Time resolved collapse of a folding protein observed with small angle x-ray scattering
    • Pollack, L., Tate, M. W., Finnefrock, A. C. et al. (2001). Time resolved collapse of a folding protein observed with small angle x-ray scattering. Phys. Rev. Lett. 86, 4962-4965.
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 4962-4965
    • Pollack, L.1    Tate, M.W.2    Finnefrock, A.C.3
  • 72
    • 0037022327 scopus 로고    scopus 로고
    • Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering
    • Akiyama, S., Takahashi, S., Kimura, T. et al. (2002). Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering. Proc. Natl Acad. Sci. USA 99, 1329-1334.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1329-1334
    • Akiyama, S.1    Takahashi, S.2    Kimura, T.3
  • 73
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands
    • Elöve, G. A., Bhuyan, A. K. & Roder, H. (1994). Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 75
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Coló n, W., Wakem, L. P., Sherman, F. & Roder, H. (1997). Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Biochemistry 36, 12535-12541.
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 76
    • 0000509513 scopus 로고    scopus 로고
    • Stopped-flow circular dichroism
    • In Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G. D., Ed.). Plenum Press, New York
    • Kuwajima, K. (1996). Stopped-flow circular dichroism. In Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G. D., Ed.). Plenum Press, New York.
    • (1996)
    • Kuwajima, K.1
  • 77
    • 0034737327 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • Hagen, S. J. & Eaton, W. A. (2000). Two-state expansion and collapse of a polypeptide. J. Mol. Biol. 297, 781-789.
    • (2000) J. Mol. Biol. , vol.297 , pp. 781-789
    • Hagen, S.J.1    Eaton, W.A.2
  • 78
    • 0030322627 scopus 로고    scopus 로고
    • Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling
    • Gladwin, S. T. & Evans, P. A. (1996). Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling. Fold. Des. 1, 407-417.
    • (1996) Fold. Des. , vol.1 , pp. 407-417
    • Gladwin, S.T.1    Evans, P.A.2
  • 79
    • 0031866483 scopus 로고    scopus 로고
    • Amide protection in an early folding intermediate of cytochrome c
    • Sauder, J. M. & Roder, H. (1998). Amide protection in an early folding intermediate of cytochrome c. Fold. Des. 3, 293-301.
    • (1998) Fold. Des. , vol.3 , pp. 293-301
    • Sauder, J.M.1    Roder, H.2
  • 80
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group exchange
    • Bai, Y., Milne, J. S. & Englander, S. W. (1993). Primary structure effects on peptide group exchange. Proteins 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Englander, S.W.3
  • 81
    • 0031205431 scopus 로고    scopus 로고
    • Protein folding pathways and intermediates
    • Clarke, A. R. & Waltho, J. P. (1997). Protein folding pathways and intermediates. Curr. Opin. Biotechnol. 8, 400-410.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 400-410
    • Clarke, A.R.1    Waltho, J.P.2
  • 82
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgGbinding domain of streptococcal protein G
    • Alexander, P., Orban, J. & Bryan, P. (1992). Kinetic analysis of folding and unfolding the 56 amino acid IgGbinding domain of streptococcal protein G. Biochemistry 31, 7243-7248.
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 83
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park, S.-H., O'Neil, K. T. & Roder, H. (1997). An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry 36, 14277-14283.
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.-H.1    O'Neil, K.T.2    Roder, H.3
  • 84
    • 0004200845 scopus 로고
    • The foundations of chemical kinetics
    • In Advanced Topics in Chemistry, 1st edn, p. 725. McGraw-Hill, New York
    • Benson, S. W. (1960). The foundations of chemical kinetics. In Advanced Topics in Chemistry, 1st edn, p. 725. McGraw-Hill, New York.
    • (1960)
    • Benson, S.W.1
  • 85
    • 0039492013 scopus 로고
    • Matrix formulation of chemical reaction rates
    • Pogliani, L. & Terenzi, M. (1992). Matrix formulation of chemical reaction rates. J. Chem. Educ. 69, 278-280.
    • (1992) J. Chem. Educ. , vol.69 , pp. 278-280
    • Pogliani, L.1    Terenzi, M.2
  • 86
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez, I. E. & Kiefhaber, T. (2003). Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325, 367-376.
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 87
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. & Nielsen, S. O. (1966). Hydrogen exchange in proteins. Adv. Protein Sci. 21, 287-386.
    • (1966) Adv. Protein Sci. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 88
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. (1968). Protein denaturation. Adv. Protein Chem. 23, 121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 89
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • Krantz, B. A., Mayne, L., Rumbley, J., Englander, S. W. & Sosnick, T. R. (2002). Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J. Mol. Biol. 324, 359-371.
    • (2002) J. Mol. Biol. , vol.324 , pp. 359-371
    • Krantz, B.A.1    Mayne, L.2    Rumbley, J.3    Englander, S.W.4    Sosnick, T.R.5
  • 90
    • 0034718524 scopus 로고    scopus 로고
    • Distinguishing between twostate and three-state models for ubiquitin folding
    • Krantz, B. A. & Sosnick, T. R. (2000). Distinguishing between twostate and three-state models for ubiquitin folding. Biochemistry 39, 11696-11701.
    • (2000) Biochemistry , vol.39 , pp. 11696-11701
    • Krantz, B.A.1    Sosnick, T.R.2
  • 91
    • 0028965952 scopus 로고
    • Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints
    • Laub, P. B., Khorasanizadeh, S. & Roder, H. (1995). Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints. Protein Sci. 4, 973-982.
    • (1995) Protein Sci. , vol.4 , pp. 973-982
    • Laub, P.B.1    Khorasanizadeh, S.2    Roder, H.3
  • 92
    • 2942617191 scopus 로고    scopus 로고
    • Is an intermediate state populated on the folding pathway of ubiquitin?
    • Went, H. M., Benitez-Cardoza, C. G. & Jackson, S. E. (2004). Is an intermediate state populated on the folding pathway of ubiquitin? FEBS Lett. 567, 333-338.
    • (2004) FEBS Lett. , vol.567 , pp. 333-338
    • Went, H.M.1    Benitez-Cardoza, C.G.2    Jackson, S.E.3
  • 93
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher, T., Chesick, J. P., Winkler, J. R. & Gray, H. B. (1996). Protein folding triggered by electron transfer. Science 271, 1558-1560.
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 94
    • 0021111761 scopus 로고
    • Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c
    • Brems, D. N. & Stellwagen, E. (1983). Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c. J. Biol. Chem. 258, 3655-3660.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3655-3660
    • Brems, D.N.1    Stellwagen, E.2
  • 95
    • 0025832142 scopus 로고
    • Effective concentrations of amino acid side chains in an unfolded protein
    • Muthukrishnan, K. & Nall, B. T. (1991). Effective concentrations of amino acid side chains in an unfolded protein. Biochemistry 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nall, B.T.2
  • 96
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidineheme ligation: Direct demonstration of a role for N-terminal amino groupheme ligation
    • Hammack, B., Godbole, S. & Bowler, B. E. (1998). Cytochrome c folding traps are not due solely to histidineheme ligation: Direct demonstration of a role for N-terminal amino groupheme ligation. J. Mol. Biol. 275, 719-724.
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 98
    • 0029964867 scopus 로고    scopus 로고
    • Diffusionlimited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S. J., Hofrichter, J., Szabo, A. & Eaton, W. A. (1996). Diffusionlimited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding. Proc. Natl Acad. Sci. USA 93, 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
  • 99
    • 0037667601 scopus 로고    scopus 로고
    • Fast chain contraction during protein folding: "foldability" and collapse dynamics
    • Qiu, L., Zachariah, C. & Hagen, S. J. (2003). Fast chain contraction during protein folding: "foldability" and collapse dynamics. Phys Rev Lett 90, 168103.
    • (2003) Phys Rev Lett , vol.90 , pp. 168103
    • Qiu, L.1    Zachariah, C.2    Hagen, S.J.3
  • 100
    • 0028929556 scopus 로고
    • Principles of protein folding-a perspective from simple exact models
    • Dill, K. A., Bromberg, S., Yue, K. et al. (1995). Principles of protein folding-a perspective from simple exact models. Protein Sci. 4, 561-602.
    • (1995) Protein Sci. , vol.4 , pp. 561-602
    • Dill, K.A.1    Bromberg, S.2    Yue, K.3
  • 101
    • 0032568599 scopus 로고    scopus 로고
    • Folding funnels and frustration in off-lattice minimalist protein landscapes
    • Nymeyer, H., Garcia, A. E. & Onuchic, J. N. (1998). Folding funnels and frustration in off-lattice minimalist protein landscapes. Proc. Natl Acad. Sci. USA 95, 5921-5928.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5921-5928
    • Nymeyer, H.1    Garcia, A.E.2    Onuchic, J.N.3
  • 102
    • 0032989351 scopus 로고    scopus 로고
    • Observation of strange kinetics in protein folding
    • Sabelko, J., Ervin, J. & Gruebele, M. (1999). Observation of strange kinetics in protein folding. Proc. Natl Acad. Sci. USA 96, 6031-6036.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6031-6036
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 103
    • 0037235662 scopus 로고    scopus 로고
    • Exponential decay kinetics in "downhill" protein folding
    • Hagen, S. J. (2003). Exponential decay kinetics in "downhill" protein folding. Proteins 50, 1-4.
    • (2003) Proteins , vol.50 , pp. 1-4
    • Hagen, S.J.1
  • 104
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space
    • Shortle, D. (2002). The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Adv. Protein Chem. 62, 1-23.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 1-23
    • Shortle, D.1
  • 105
    • 0000697562 scopus 로고
    • Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford, C., Kawahara, K. & Lapanje, S. (1967). Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J. Am. Chem. Soc. 89, 729-749.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 729-749
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 106
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: the rate-limiting step in twostate cytochrome c folding
    • Sosnick, T. R., Mayne, L. & Englander, S. W. (1996). Molecular collapse: the rate-limiting step in twostate cytochrome c folding. Proteins 24, 413-426.
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 108
    • 0031697733 scopus 로고    scopus 로고
    • The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
    • Qi, P. X., Sosnick, T. R. & Englander, S. W. (1998). The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Struct. Biol. 5, 882-884.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 882-884
    • Qi, P.X.1    Sosnick, T.R.2    Englander, S.W.3
  • 109
    • 0032514727 scopus 로고    scopus 로고
    • Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores
    • Choe, S. E., Matsudaira, P. T., Osterhout, J., Wagner, G. & Shakhnovich, E. I. (1998). Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry 37, 14508-14518.
    • (1998) Biochemistry , vol.37 , pp. 14508-14518
    • Choe, S.E.1    Matsudaira, P.T.2    Osterhout, J.3    Wagner, G.4    Shakhnovich, E.I.5
  • 110
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • Ferguson, N., Capaldi, A. P., James, R., Kleanthous, C. & Radford, S. E. (1999). Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J. Mol. Biol. 286, 1597-1608.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 111
    • 0035965128 scopus 로고    scopus 로고
    • Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9
    • Gorski, S. A., Capaldi, A. P., Kleanthous, C. & Radford, S. E. (2001). Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9. J. Mol. Biol. 312, 849-863.
    • (2001) J. Mol. Biol. , vol.312 , pp. 849-863
    • Gorski, S.A.1    Capaldi, A.P.2    Kleanthous, C.3    Radford, S.E.4
  • 113
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric l repressor
    • Huang, G. S. & Oas, T. G. (1995). Submillisecond folding of monomeric l repressor. Proc. Natl Acad. Sci. USA 92, 6878-6882.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 115
    • 0033535839 scopus 로고    scopus 로고
    • Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a fourhelix-bundle protein
    • Wittung-Stafshede, P., Lee, J. C., Winkler, J. R. & Gray, H. B. (1999). Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a fourhelix-bundle protein. Proc. Natl Acad. Sci. USA 96, 6587-6590.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6587-6590
    • Wittung-Stafshede, P.1    Lee, J.C.2    Winkler, J.R.3    Gray, H.B.4
  • 116
    • 0033537683 scopus 로고    scopus 로고
    • Microsecond folding of the cold shock protein measured by a pressure-jump technique
    • Jacob, M., Holtermann, G., Perl, D. et al. (1999). Microsecond folding of the cold shock protein measured by a pressure-jump technique. Biochemistry 38, 2882-2891.
    • (1999) Biochemistry , vol.38 , pp. 2882-2891
    • Jacob, M.1    Holtermann, G.2    Perl, D.3
  • 117
    • 0028402735 scopus 로고
    • The energetic ups and downs of protein folding
    • Creighton, T. E. (1994). The energetic ups and downs of protein folding. Nature Struct. Biol. 1, 135-138.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 135-138
    • Creighton, T.E.1
  • 118
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. (1995). Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA 92, 10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 119
    • 0002775727 scopus 로고
    • Early stages of protein folding
    • In Mechanisms of Protein Folding: Frontiers in Molecular Biology (Pain, R. H., Ed.), Oxford University Press, New York
    • Roder, H. & Elöve, G. A. (1994). Early stages of protein folding. In Mechanisms of Protein Folding: Frontiers in Molecular Biology (Pain, R. H., Ed.), pp. 26-55. Oxford University Press, New York.
    • (1994) , pp. 26-55
    • Roder, H.1    Elöve, G.A.2
  • 120
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow, M. & Oliveberg, M. (1997). Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl Acad. Sci. USA 94, 6084-6086.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 121
    • 0039825244 scopus 로고
    • Analysis of protein folding by protein engineering
    • In Mechanisms of Protein Folding: Frontiers in Molecular Biology (Pain, R. H., Ed.), Oxford University Press, Oxford
    • Matouschek, A., Serrano, L. & Fersht, A. R. (1994). Analysis of protein folding by protein engineering. In Mechanisms of Protein Folding: Frontiers in Molecular Biology (Pain, R. H., Ed.), pp. 137-159. Oxford University Press, Oxford.
    • (1994) , pp. 137-159
    • Matouschek, A.1    Serrano, L.2    Fersht, A.R.3
  • 122
    • 0032884925 scopus 로고    scopus 로고
    • Confirmation of the hierarchical folding of RNase H: a protein engineering study
    • Raschke, T. M., Kho, J. & Marqusee, S. (1999). Confirmation of the hierarchical folding of RNase H: a protein engineering study. Nature Struct. Biol. 6, 825-831.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 825-831
    • Raschke, T.M.1    Kho, J.2    Marqusee, S.3
  • 123
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in Staphylococcal nuclease
    • Walkenhorst, W. F., Green, S. M. & Roder, H. (1997). Kinetic evidence for folding and unfolding intermediates in Staphylococcal nuclease. Biochemistry 63, 5795-5805.
    • (1997) Biochemistry , vol.63 , pp. 5795-5805
    • Walkenhorst, W.F.1    Green, S.M.2    Roder, H.3
  • 124
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber, T. (1995). Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA 92, 9029-9033.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 125
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1b
    • Heidary, D. K., Gross, L. A., Roy, M. & Jennings, P. A. (1997). Evidence for an obligatory intermediate in the folding of interleukin-1b. Nature Struct. Biol. 4, 725-731.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 127
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate
    • Tsui, V., Garcia, C., Cavagnero, S., Siuzdak, G., Dyson, H. J. & Wright, P. E. (1999). Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate. Protein Sci. 8, 45-49.
    • (1999) Protein Sci. , vol.8 , pp. 45-49
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 128
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: misfolding on a path to the native state
    • Capaldi, A. P., Kleanthous, C. & Radford, S. E. (2002). Im7 folding mechanism: misfolding on a path to the native state. Nature Struct. Biol. 9, 209-216.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 129
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T. & Baker, D. (1998). Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 130
    • 0035005366 scopus 로고    scopus 로고
    • Preorganized secondary structure as an important determinant of fast protein folding
    • Myers, J. K. & Oas, T. G. (2001). Preorganized secondary structure as an important determinant of fast protein folding. Nature Struct. Biol. 8, 552-558.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 552-558
    • Myers, J.K.1    Oas, T.G.2
  • 131
    • 0037032225 scopus 로고    scopus 로고
    • Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros
    • Qiu, L., Pabit, S. A., Roitberg, A. E. & Hagen, S. J. (2002). Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J. Am. Chem. Soc. 124, 12952-12953.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12952-12953
    • Qiu, L.1    Pabit, S.A.2    Roitberg, A.E.3    Hagen, S.J.4
  • 132
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • Mayor, U., Guydosh, N. R., Johnson, C. M. et al. (2003). The complete folding pathway of a protein from nanoseconds to microseconds. Nature 421, 863-867.
    • (2003) Nature , vol.421 , pp. 863-867
    • Mayor, U.1    Guydosh, N.R.2    Johnson, C.M.3
  • 133
    • 0346734133 scopus 로고    scopus 로고
    • Ultrafast folding of alpha3D: a de novo designed threehelix bundle protein
    • Zhu, Y., Alonso, D. O., Maki, K. et al. (2003). Ultrafast folding of alpha3D: a de novo designed threehelix bundle protein. Proc. Natl Acad. Sci. USA 100, 15486-15491.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15486-15491
    • Zhu, Y.1    Alonso, D.O.2    Maki, K.3
  • 134
    • 0025685902 scopus 로고
    • Time-resolved fluorescence studies of the protein folding process: new instrumentation, analysis and experimental approaches in timeresolved laser spectroscopy in biochemistry
    • Beechem, J. M., James, L. & Brand, L. (1990). Time-resolved fluorescence studies of the protein folding process: new instrumentation, analysis and experimental approaches in timeresolved laser spectroscopy in biochemistry. SPIE Proc. 1204, 686-698.
    • (1990) SPIE Proc. , vol.1204 , pp. 686-698
    • Beechem, J.M.1    James, L.2    Brand, L.3
  • 135
    • 0028925815 scopus 로고
    • Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy
    • Jones, B. E., Beechem, J. M. & Matthews, C. R. (1995). Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry 34, 1867-1877.
    • (1995) Biochemistry , vol.34 , pp. 1867-1877
    • Jones, B.E.1    Beechem, J.M.2    Matthews, C.R.3
  • 137
    • 0242286689 scopus 로고    scopus 로고
    • The kinetics of side chain stabilization during protein folding
    • Frieden, C. (2003). The kinetics of side chain stabilization during protein folding. Biochemistry 42, 12439-12446.
    • (2003) Biochemistry , vol.42 , pp. 12439-12446
    • Frieden, C.1
  • 138
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in Lysozyme folding with time resolved small-angle X-ray scattering
    • Segel, D. J., Bachmann, A., Hofrichter, J., Hodgson, K. O., Doniach, S. & Kiefhaber, T. (1999). Characterization of transient intermediates in Lysozyme folding with time resolved small-angle X-ray scattering. J. Mol. Biol. 288, 489-499.
    • (1999) J. Mol. Biol. , vol.288 , pp. 489-499
    • Segel, D.J.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.O.4    Doniach, S.5    Kiefhaber, T.6
  • 139
    • 0024726838 scopus 로고
    • Determination of the dead time of a stopped-flow fluorometer
    • Brissette, P., Ballou, D. P. & Massey, V. (1989). Determination of the dead time of a stopped-flow fluorometer. Anal. Biochem. 181, 234-238.
    • (1989) Anal. Biochem. , vol.181 , pp. 234-238
    • Brissette, P.1    Ballou, D.P.2    Massey, V.3
  • 140
    • 0345562799 scopus 로고
    • Kinetics of heme-protein intractions
    • In Hemes and Hemeproteins (Chance, B., Estabrook, R. W. & Yonetani, T., Eds), Academic Press, New York
    • Gibson, Q. H. & Antonini, E. (1966). Kinetics of heme-protein intractions. In Hemes and Hemeproteins (Chance, B., Estabrook, R. W. & Yonetani, T., Eds), pp. 67-78. Academic Press, New York.
    • (1966) , pp. 67-78
    • Gibson, Q.H.1    Antonini, E.2
  • 142
    • 0001564815 scopus 로고
    • Meth
    • Gutfreund, H. (1969). Meth. Enzymol. 16, 229-249.
    • (1969) Enzymol. , vol.16 , pp. 229-249
    • Gutfreund, H.1
  • 143
    • 0028902628 scopus 로고
    • Microsecond generation of oxygenbound cytochrome c oxidase by rapid solution mixing
    • Takahashi, S., Ching, Y.-c., Wang, J. & Rousseau, D. L. (1995). Microsecond generation of oxygenbound cytochrome c oxidase by rapid solution mixing. J. Biol. Chem. 270, 8405-8407.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8405-8407
    • Takahashi, S.1    Ching, Y.-C.2    Wang, J.3    Rousseau, D.L.4
  • 144
    • 84996308561 scopus 로고
    • Time-resolved resonance raman spectroscopy using a fast mixing device
    • Paeng, K., Paeng, I. & Kincaid, J. (1994). Time-resolved resonance raman spectroscopy using a fast mixing device. Anal. Sci. 10, 157-159.
    • (1994) Anal. Sci. , vol.10 , pp. 157-159
    • Paeng, K.1    Paeng, I.2    Kincaid, J.3
  • 145
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher, T., Alexander, P., Bryan, P. & Gilliland, G. L. (1994). Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33, 4721-4729.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 146
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G. W., Louie, G. V. & Brayer, G. D. (1990). High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214, 585-595.
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3


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