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Volumn 101-102, Issue , 2002, Pages 113-131

Sequential vs. parallel protein-folding mechanisms: Experimental tests for complex folding reactions

Author keywords

Absorbance; Fluorescence; Kinetics; Spectroscopy

Indexed keywords

CYTOCHROME C; DIHYDROFOLATE REDUCTASE; HYDROGEN; INTERLEUKIN 1BETA; LYSOZYME; TRYPTOPHAN SYNTHASE;

EID: 0037058950     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00155-2     Document Type: Article
Times cited : (54)

References (128)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding? J. Chem. Phys. 65:1968;44-45.
    • (1968) J. Chem. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 3
    • 0032744232 scopus 로고    scopus 로고
    • Protein folding: From the Levinthal paradox to structure prediction
    • Honig B. Protein folding: from the Levinthal paradox to structure prediction. J. Mol. Biol. 293:1999;283-293.
    • (1999) J. Mol. Biol. , vol.293 , pp. 283-293
    • Honig, B.1
  • 4
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews C.R. Pathways of protein folding. Annu. Rev. Biochem. 62:1993;653-683.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 5
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 6
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson C.M., Sali A., Karplus M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37:1998;868-893.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 7
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • Alm E., Baker D. Matching theory and experiment in protein folding. Curr. Opin. Struct. Biol. 9:1999;189-196.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 8
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin R.L., Rose G.D. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem. Sci. 24:1999;26-33.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 9
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin R.L., Rose G.D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24:1999;77-83.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 10
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson C.M., Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9:1999;92-101.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 11
  • 12
    • 0034581629 scopus 로고    scopus 로고
    • Barriers in protein folding reactions
    • Bilsel O., Matthews C.R. Barriers in protein folding reactions. Adv. Prot. Chem. 53:2000;153-207.
    • (2000) Adv. Prot. Chem. , vol.53 , pp. 153-207
    • Bilsel, O.1    Matthews, C.R.2
  • 14
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers H.A. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica. 7:1940;284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 18
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios
    • Onuchic J.N., Nymeyer H., Garcia A.E., Chahine J., Socci N.D. The energy landscape theory of protein folding: insights into folding mechanisms and scenarios. Adv. Protein Chem. 53:2000;87-152.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 87-152
    • Onuchic, J.N.1    Nymeyer, H.2    Garcia, A.E.3    Chahine, J.4    Socci, N.D.5
  • 19
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R.L. On-pathway versus off-pathway folding intermediates. Fold. Des. 1:1996;R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 20
    • 0030735983 scopus 로고    scopus 로고
    • Competing unfolding pathways
    • Baldwin R.L. Competing unfolding pathways. Nature Struct. Biol. 4:1997;965-966.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 965-966
    • Baldwin, R.L.1
  • 22
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models of protein folding kinetics
    • Zwanzig R. Two-state models of protein folding kinetics. Proc. Natl. Acad. Sci. USA. 94:1997;148-150.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 148-150
    • Zwanzig, R.1
  • 24
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Protein Chem. 23:1968;121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 25
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1970;1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 26
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins I. Mathematical analysis
    • Ikai A., Tanford C. Kinetics of unfolding and refolding of proteins I. Mathematical analysis. J. Mol. Biol. 73:1973;145-163.
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2
  • 27
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P.S., Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 28
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S.E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 30
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein Escherichia coli CspA
    • Reid K.L., Rodriguez H.M., Hillier B.J., Gregoret L.M. Stability and folding properties of a model beta-sheet protein Escherichia coli CspA. Protein Sci. 7:1998;470-479.
    • (1998) Protein Sci. , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    Hillier, B.J.3    Gregoret, L.M.4
  • 31
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson S.E., Fersht A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry. 30:1991;10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 32
    • 0017282561 scopus 로고
    • A quantitative treatment of the kinetics of the folding transition of ribonuclease A
    • Hagerman P.J., Baldwin R.L. A quantitative treatment of the kinetics of the folding transition of ribonuclease A. Biochemistry. 15:1976;1462-1473.
    • (1976) Biochemistry , vol.15 , pp. 1462-1473
    • Hagerman, P.J.1    Baldwin, R.L.2
  • 33
    • 0017399699 scopus 로고
    • A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism
    • Kuwajima K. A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism. J. Mol. Biol. 114:1977;241-258.
    • (1977) J. Mol. Biol. , vol.114 , pp. 241-258
    • Kuwajima, K.1
  • 34
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S.E., Dobson C.M., Evans P.A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 35
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson C.M., Evans P.A., Radford S.E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19:1994;31-37.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 36
    • 0023055739 scopus 로고
    • Folding of dihydrofolate reductase from Escherichia coli
    • Touchette N.A., Perry K.M., Matthews C.R. Folding of dihydrofolate reductase from Escherichia coli. Biochemistry. 25:1986;5445-5452.
    • (1986) Biochemistry , vol.25 , pp. 5445-5452
    • Touchette, N.A.1    Perry, K.M.2    Matthews, C.R.3
  • 37
    • 0025373255 scopus 로고
    • Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites
    • Frieden C. Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites. Proc. Natl. Acad. Sci. USA. 87:1990;4413-4416.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4413-4416
    • Frieden, C.1
  • 38
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings P.A., Finn B.E., Jones B.E., Matthews C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry. 32:1993;3783-3789.
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 39
    • 0028561835 scopus 로고
    • Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
    • Jones B.E., Jennings P.A., Pierre R.A., Matthews C.R. Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry. 33:1994;15250-15258.
    • (1994) Biochemistry , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre, R.A.3    Matthews, C.R.4
  • 40
    • 0028947956 scopus 로고
    • Early intermediate in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones B.E., Matthews C.R. Early intermediate in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 4:1995;167-177.
    • (1995) Protein Sci. , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 41
    • 0019890114 scopus 로고
    • Characterization of the slow steps in the folding of the α subunit of tryptophan synthase
    • Crisanti M.M., Matthews C.R. Characterization of the slow steps in the folding of the α subunit of tryptophan synthase. Biochemistry. 20:1981;2700-2706.
    • (1981) Biochemistry , vol.20 , pp. 2700-2706
    • Crisanti, M.M.1    Matthews, C.R.2
  • 42
    • 0033579862 scopus 로고    scopus 로고
    • Folding mechanism of the alpha-subunit of tryptophan synthase, an α/β barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels
    • Bilsel O., Zitzewitz J.A., Bowers K.E., Matthews C.R. Folding mechanism of the alpha-subunit of tryptophan synthase, an α/β barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 38:1999;1018-1029.
    • (1999) Biochemistry , vol.38 , pp. 1018-1029
    • Bilsel, O.1    Zitzewitz, J.A.2    Bowers, K.E.3    Matthews, C.R.4
  • 43
    • 0033060003 scopus 로고    scopus 로고
    • Identifying the structural boundaries of independent folding domains in the α/β barrel protein, α tryptophan synthase
    • Zitzewitz J.A., Gualfetti P.J., Perkons I.E., Wasta S.A., Matthews C.R. Identifying the structural boundaries of independent folding domains in the α/β barrel protein, α tryptophan synthase. Protein Sci. 8:1999;1200-1209.
    • (1999) Protein Sci. , vol.8 , pp. 1200-1209
    • Zitzewitz, J.A.1    Gualfetti, P.J.2    Perkons, I.E.3    Wasta, S.A.4    Matthews, C.R.5
  • 44
    • 0025334690 scopus 로고
    • Folding and stability of Trp aporepressor from Escherichia coli
    • Gittelman M.S., Matthews C.R. Folding and stability of Trp aporepressor from Escherichia coli. Biochemistry. 29:1990;7011-7020.
    • (1990) Biochemistry , vol.29 , pp. 7011-7020
    • Gittelman, M.S.1    Matthews, C.R.2
  • 45
    • 0027190920 scopus 로고
    • Structure and stability of an early folding intermediate of Escherichia coli Trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
    • Mann C.J., Matthews C.R. Structure and stability of an early folding intermediate of Escherichia coli Trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry. 32:1993;5282-5290.
    • (1993) Biochemistry , vol.32 , pp. 5282-5290
    • Mann, C.J.1    Matthews, C.R.2
  • 46
    • 0028810468 scopus 로고
    • Characterization of the slow folding reactions of Trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase
    • Mann C.J., Shao X., Matthews C.R. Characterization of the slow folding reactions of Trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry. 34:1995;14573-14580.
    • (1995) Biochemistry , vol.34 , pp. 14573-14580
    • Mann, C.J.1    Shao, X.2    Matthews, C.R.3
  • 47
    • 0032506048 scopus 로고    scopus 로고
    • Mechanism of folding of the dimeric core domain of Escherichia coli Trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate
    • Gloss L.M., Matthews C.R. Mechanism of folding of the dimeric core domain of Escherichia coli Trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry. 37:1998;15990-15999.
    • (1998) Biochemistry , vol.37 , pp. 15990-15999
    • Gloss, L.M.1    Matthews, C.R.2
  • 48
    • 0032506169 scopus 로고    scopus 로고
    • The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions
    • Gloss L.M., Matthews C.R. The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry. 37:1998;16000-16010.
    • (1998) Biochemistry , vol.37 , pp. 16000-16010
    • Gloss, L.M.1    Matthews, C.R.2
  • 49
    • 0035812633 scopus 로고    scopus 로고
    • Rough energy landscapes in protein folding: Dimeric E. coli Trp repressor folds through three parallel channels
    • Gloss L.M., Simler B.R., Matthews C.R. Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. J. Mol. Biol. 312:2001;1121-1134.
    • (2001) J. Mol. Biol. , vol.312 , pp. 1121-1134
    • Gloss, L.M.1    Simler, B.R.2    Matthews, C.R.3
  • 51
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger G., Kiefhaber T. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270:1997;294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 52
    • 0035909813 scopus 로고    scopus 로고
    • Apoflavodoxin folding mechanism: An α/β protein with an essentially off-pathway intermediate
    • Fernandez-Recio J., Genzor C.G., Sancho J. Apoflavodoxin folding mechanism: an α/β protein with an essentially off-pathway intermediate. Biochemistry. 40:2001;15234-15245.
    • (2001) Biochemistry , vol.40 , pp. 15234-15245
    • Fernandez-Recio, J.1    Genzor, C.G.2    Sancho, J.3
  • 53
    • 0022555910 scopus 로고
    • Kinetic mechanisms of protein folding
    • Utiyama H., Baldwin R.L. Kinetic mechanisms of protein folding. Methods Enzymol. 131:1986;51-70.
    • (1986) Methods Enzymol. , vol.131 , pp. 51-70
    • Utiyama, H.1    Baldwin, R.L.2
  • 54
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews C.R. Effect of point mutations on the folding of globular proteins. Methods Enzymol. 154:1987;498-511.
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 55
    • 0029130877 scopus 로고
    • Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins
    • Eftink M.R. Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins. Methods Enzymol. 259:1995;487-512.
    • (1995) Methods Enzymol. , vol.259 , pp. 487-512
    • Eftink, M.R.1
  • 56
    • 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. A continuous-flow capillary mixer to monitor reactions on the microsecond time scale. Biophys. J. 74:1998;2714-2721.
    • (1998) Biophys. J. , vol.74 , pp. 2714-2721
    • Shastry, M.C.R.1    Luck, S.D.2    Roder, H.3
  • 57
    • 0032844656 scopus 로고    scopus 로고
    • Methods for exploring early events in protein folding
    • Roder H., Shastry M.R. Methods for exploring early events in protein folding. Curr. Opin. Struct. Biol. 9:1999;620-626.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 620-626
    • Roder, H.1    Shastry, M.R.2
  • 58
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' mode
    • 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' mode. Biochemistry. 36:1997;9200-9210.
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 62
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman J.A. Solvent denaturation. Biopolymers. 17:1978;1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 63
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - A flexible, portable system
    • Barshop B.A., Wrenn R.F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM - a flexible, portable system. Anal. Biochem. 130:1983;134-145.
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 64
    • 0030792287 scopus 로고    scopus 로고
    • New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM
    • Dang Q., Frieden C. New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM. Trends Biochem. Sci. 22:1997;317.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 317
    • Dang, Q.1    Frieden, C.2
  • 65
    • 0022323072 scopus 로고
    • Slow refolding kinetics in yeast iso-2 cytochrome c
    • Osterhout J.J. Jr., Nall B.T. Slow refolding kinetics in yeast iso-2 cytochrome c. Biochemistry. 24:1985;7999-8005.
    • (1985) Biochemistry , vol.24 , pp. 7999-8005
    • Osterhout J.J., Jr.1    Nall, B.T.2
  • 66
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi F.N., Nath U., Udgaonkar J.B. Multiple intermediates and transition states during protein unfolding. Nature Struct. Biol. 4:1997;1016-1024.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 1016-1024
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 67
    • 0021113912 scopus 로고
    • Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates
    • Schmid F.X. Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry. 22:1983;4690-4696.
    • (1983) Biochemistry , vol.22 , pp. 4690-4696
    • Schmid, F.X.1
  • 68
    • 0034685611 scopus 로고    scopus 로고
    • Coupled kinetic traps in cytochrome c folding: His-Heme misligation and proline isomerization
    • Pierce M.M., Nall B.T. Coupled kinetic traps in cytochrome c folding: His-Heme misligation and proline isomerization. J. Mol. Biol. 298:2000;955-969.
    • (2000) J. Mol. Biol. , vol.298 , pp. 955-969
    • Pierce, M.M.1    Nall, B.T.2
  • 69
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P.S., Baldwin R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:1982;459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 70
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H., Colon W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:1997;15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 72
    • 0036289101 scopus 로고    scopus 로고
    • Highly divergent dihydrofolate reductases conserve complex folding mechanisms
    • Wallace L.A., Matthews C.R. Highly divergent dihydrofolate reductases conserve complex folding mechanisms. J. Mol. Biol. 315:2002;193-211.
    • (2002) J. Mol. Biol. , vol.315 , pp. 193-211
    • Wallace, L.A.1    Matthews, C.R.2
  • 73
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1 beta
    • Heidary D.K., Gross L.A., Roy M., Jennings P.A. Evidence for an obligatory intermediate in the folding of interleukin-1 beta. Nature Struct. Biol. 4:1997;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
  • 74
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder H., Elove G.A., Englander S.W. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature. 335:1988;700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elove, G.A.2    Englander, S.W.3
  • 75
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar J.B., Baldwin R.L. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 335:1988;694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 76
    • 0024331090 scopus 로고
    • Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
    • Roder H. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol. 176:1989;446-473.
    • (1989) Methods Enzymol. , vol.176 , pp. 446-473
    • Roder, H.1
  • 77
    • 0031908874 scopus 로고    scopus 로고
    • Hydrogen exchange studies of protein structure
    • Raschke T.M., Marqusee S. Hydrogen exchange studies of protein structure. Curr. Opin. Biotech. 9:1998;80-86.
    • (1998) Curr. Opin. Biotech. , vol.9 , pp. 80-86
    • Raschke, T.M.1    Marqusee, S.2
  • 78
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstom-Lang
    • Englander S.W., Mayne L., Bai Y., Sosnick T.R. Hydrogen exchange: the modern legacy of Linderstom-Lang. Protein Sci. 6:1997;1101-1109.
    • (1997) Protein Sci. , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 79
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander S.W. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 29:2000;213-238.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 81
    • 0017845745 scopus 로고
    • Kinetics of ligand binding to dihydrofolate reductase: Binary complex formation with NADPH and coenzyme analogues
    • Dunn S.M., Batchelor J.G., King R.W. Kinetics of ligand binding to dihydrofolate reductase: binary complex formation with NADPH and coenzyme analogues. Biochemistry. 17:1978;2356-2364.
    • (1978) Biochemistry , vol.17 , pp. 2356-2364
    • Dunn, S.M.1    Batchelor, J.G.2    King, R.W.3
  • 82
    • 0019328545 scopus 로고
    • Kinetics of ternary complex formation between dihydrofolate reductase, coenzyme, and inhibitors
    • Dunn S.M., King R.W. Kinetics of ternary complex formation between dihydrofolate reductase, coenzyme, and inhibitors. Biochemistry. 19:1980;766-773.
    • (1980) Biochemistry , vol.19 , pp. 766-773
    • Dunn, S.M.1    King, R.W.2
  • 83
    • 0023860769 scopus 로고
    • Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase
    • Taira K., Benkovic S.J. Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase. J. Med. Chem. 31:1988;129-137.
    • (1988) J. Med. Chem. , vol.31 , pp. 129-137
    • Taira, K.1    Benkovic, S.J.2
  • 84
    • 0033613814 scopus 로고    scopus 로고
    • Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures
    • Clarke C., Frieden C. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J. Mol. Biol. 285:1999;1765-1776.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1765-1776
    • Clarke, C.1    Frieden, C.2
  • 85
    • 0034622508 scopus 로고    scopus 로고
    • Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
    • Ionescu R.M., Smith V.F., O'Neill J.C. Jr., Matthews C.R. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry. 39:2000;9540-9550.
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.M.1    Smith, V.F.2    O'Neill J.C., Jr.3    Matthews, C.R.4
  • 86
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts J.F., Halvorson H.R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry. 14:1975;4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 87
    • 0021103614 scopus 로고
    • Effect of a single amino acid substitution on the folding of the a subunit of tryptophan synthase
    • Matthews C.R., Crisanti M.M., Manz J.T., Gepner G.L. Effect of a single amino acid substitution on the folding of the a subunit of tryptophan synthase. Biochemistry. 22:1983;1445-1452.
    • (1983) Biochemistry , vol.22 , pp. 1445-1452
    • Matthews, C.R.1    Crisanti, M.M.2    Manz, J.T.3    Gepner, G.L.4
  • 88
    • 0023203755 scopus 로고
    • Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli
    • Hurle M.R., Matthews C.R. Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli. Biochim. Biophys. Acta. 913:1987;179-184.
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 179-184
    • Hurle, M.R.1    Matthews, C.R.2
  • 90
    • 0025105230 scopus 로고
    • Multiple replacements at position 211 in the α subunit of tryptophan synthase as a probe of the folding unit association reaction
    • Tweedy N.B., Hurle M.R., Chrunyk B.A., Matthews C.R. Multiple replacements at position 211 in the α subunit of tryptophan synthase as a probe of the folding unit association reaction. Biochemistry. 29:1990;1539-1545.
    • (1990) Biochemistry , vol.29 , pp. 1539-1545
    • Tweedy, N.B.1    Hurle, M.R.2    Chrunyk, B.A.3    Matthews, C.R.4
  • 91
    • 0033520098 scopus 로고    scopus 로고
    • Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein
    • Zitzewitz J.A., Matthews C.R. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry. 38:1999;10205-10214.
    • (1999) Biochemistry , vol.38 , pp. 10205-10214
    • Zitzewitz, J.A.1    Matthews, C.R.2
  • 92
    • 0028258789 scopus 로고
    • Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements
    • Ogasahara K., Yutani K. Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements. J. Mol. Biol. 236:1994;1227-1240.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1227-1240
    • Ogasahara, K.1    Yutani, K.2
  • 93
    • 0031039381 scopus 로고    scopus 로고
    • Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit
    • Ogasahara K., Yutani K. Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. Biochemistry. 36:1997;932-940.
    • (1997) Biochemistry , vol.36 , pp. 932-940
    • Ogasahara, K.1    Yutani, K.2
  • 94
    • 0019883139 scopus 로고
    • Urea-induced unfolding of the α subunit of tryptophan synthase: Evidence for a multistate process
    • Matthews C.R., Crisanti M.M. Urea-induced unfolding of the α subunit of tryptophan synthase: evidence for a multistate process. Biochemistry. 20:1981;784-792.
    • (1981) Biochemistry , vol.20 , pp. 784-792
    • Matthews, C.R.1    Crisanti, M.M.2
  • 95
    • 0032813944 scopus 로고    scopus 로고
    • The progressive development of structure and stability during the folding of the a subunit of tryptophan synthase from E. coli
    • Gualfetti P.J., Bilsel O., Matthews C.R. The progressive development of structure and stability during the folding of the a subunit of tryptophan synthase from E. coli. Protein Sci. 8:1999;1623-1635.
    • (1999) Protein Sci. , vol.8 , pp. 1623-1635
    • Gualfetti, P.J.1    Bilsel, O.2    Matthews, C.R.3
  • 96
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick T.R., Mayne L., Englander S.W. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins Struct. Funct. Genet. 24:1996;413-426.
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 97
    • 0028818785 scopus 로고
    • A kinetic explanation for the rearrangement pathway of BPTI folding
    • Weissman J.S., Kim P.S. A kinetic explanation for the rearrangement pathway of BPTI folding. Nature Struct. Biol. 2:1995;1123-1130.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1123-1130
    • Weissman, J.S.1    Kim, P.S.2
  • 98
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya M.R., Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 36:1997;586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 99
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K., Garvey E.P., Finn B.E., Matthews C.R., Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry. 30:1991;7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 100
    • 0034723140 scopus 로고    scopus 로고
    • Localized, stereochemically-sensitive hydrophobic packing in an early intermediate of dihydrofolate reductase of Escherichia coli
    • O'Neill J.C. Jr., Matthews C.R. Localized, stereochemically-sensitive hydrophobic packing in an early intermediate of dihydrofolate reductase of Escherichia coli. J. Mol. Biol. 295:2000;737-744.
    • (2000) J. Mol. Biol. , vol.295 , pp. 737-744
    • O'Neill J.C., Jr.1    Matthews, C.R.2
  • 101
    • 0028901085 scopus 로고
    • The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates
    • Shastry M.C., Udgaonkar J.B. The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates. J. Mol. Biol. 247:1995;1013-1027.
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013-1027
    • Shastry, M.C.1    Udgaonkar, J.B.2
  • 102
    • 0035909818 scopus 로고    scopus 로고
    • PH-jump-induced folding and unfolding studies of barstar: Evidence for multiple folding and unfolding pathways
    • Rami B.R., Udgaonkar J.B. pH-jump-induced folding and unfolding studies of barstar: evidence for multiple folding and unfolding pathways. Biochemistry. 40:2001;15267-15279.
    • (2001) Biochemistry , vol.40 , pp. 15267-15279
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 103
    • 0027385015 scopus 로고
    • The refolding of cis- and trans-peptidylprolyl isomers of barstar
    • Schreiber G., Fersht A.R. The refolding of cis- and trans-peptidylprolyl isomers of barstar. Biochemistry. 32:1993;11195-11203.
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 104
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA. 92:1995;9029-9033.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 105
    • 0017189603 scopus 로고
    • The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides
    • Grathwohl C., Wuthrich K. The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides. Biopolymers. 15:1976;2025-2041.
    • (1976) Biopolymers , vol.15 , pp. 2025-2041
    • Grathwohl, C.1    Wuthrich, K.2
  • 106
    • 0025195733 scopus 로고
    • Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
    • Kiefhaber T., Quaas R., Hahn U., Schmid F.X. Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry. 29:1990;3053-3061.
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 107
    • 0029868655 scopus 로고    scopus 로고
    • Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique
    • Mayr L.M., Odefey C., Schutkowski M., Schmid F.X. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry. 35:1996;5550-5561.
    • (1996) Biochemistry , vol.35 , pp. 5550-5561
    • Mayr, L.M.1    Odefey, C.2    Schutkowski, M.3    Schmid, F.X.4
  • 108
    • 0025923291 scopus 로고
    • The Pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding-folding kinetics
    • Kuwajima K., Okayama N., Yamamoto K., Ishihara T., Sugai S. The Pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding-folding kinetics. FEBS Lett. 290:1991;135-138.
    • (1991) FEBS Lett. , vol.290 , pp. 135-138
    • Kuwajima, K.1    Okayama, N.2    Yamamoto, K.3    Ishihara, T.4    Sugai, S.5
  • 109
    • 0022471054 scopus 로고
    • Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxin
    • Kelley R.F., Wilson J., Bryant C., Stellwagen E. Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxin. Biochemistry. 25:1986;728-732.
    • (1986) Biochemistry , vol.25 , pp. 728-732
    • Kelley, R.F.1    Wilson, J.2    Bryant, C.3    Stellwagen, E.4
  • 110
    • 0030019644 scopus 로고    scopus 로고
    • Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A
    • Dodge R.W., Scheraga H.A. Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A. Biochemistry. 35:1996;1548-1559.
    • (1996) Biochemistry , vol.35 , pp. 1548-1559
    • Dodge, R.W.1    Scheraga, H.A.2
  • 111
    • 0029846913 scopus 로고    scopus 로고
    • Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A
    • Sendak R.A., Rothwarf D.M., Wedemeyer W.J., Houry W.A., Scheraga H.A. Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A. Biochemistry. 35:1996;12978-12992.
    • (1996) Biochemistry , vol.35 , pp. 12978-12992
    • Sendak, R.A.1    Rothwarf, D.M.2    Wedemeyer, W.J.3    Houry, W.A.4    Scheraga, H.A.5
  • 112
    • 0022555898 scopus 로고
    • Fast-folding and slow-folding forms of unfolded proteins
    • Schmid F.X. Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol. 131:1986;70-82.
    • (1986) Methods Enzymol. , vol.131 , pp. 70-82
    • Schmid, F.X.1
  • 113
    • 0019406826 scopus 로고
    • A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A
    • Schmid F.X., Blaschek H. A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. Eur. J. Biochem. 114:1981;111-117.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 111-117
    • Schmid, F.X.1    Blaschek, H.2
  • 114
    • 0018759051 scopus 로고
    • Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase
    • Williams J.W., Morrison J.F., Duggleby R.G. Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase. Biochemistry. 18:1979;2567-2573.
    • (1979) Biochemistry , vol.18 , pp. 2567-2573
    • Williams, J.W.1    Morrison, J.F.2    Duggleby, R.G.3
  • 115
    • 0026013162 scopus 로고
    • Demonstration by NMR of folding domains in lysozyme
    • Miranker A., Radford S.E., Karplus M., Dobson C.M. Demonstration by NMR of folding domains in lysozyme. Nature. 349:1991;633-636.
    • (1991) Nature , vol.349 , pp. 633-636
    • Miranker, A.1    Radford, S.E.2    Karplus, M.3    Dobson, C.M.4
  • 116
    • 0024995943 scopus 로고
    • Detection and characterization of a folding intermediate in barnase by NMR
    • Bycroft M., Matouschek A., Kellis J.T.J., Serrano L., Fersht A.R. Detection and characterization of a folding intermediate in barnase by NMR. Nature. 346:1990;488-490.
    • (1990) Nature , vol.346 , pp. 488-490
    • Bycroft, M.1    Matouschek, A.2    Kellis, J.T.J.3    Serrano, L.4    Fersht, A.R.5
  • 117
    • 0020475131 scopus 로고
    • Identification and characterization of the direct folding process of hen egg-white lysozyme
    • Kato S., Shimamoto N., Utiyama H. Identification and characterization of the direct folding process of hen egg-white lysozyme. Biochemistry. 21:1982;38-43.
    • (1982) Biochemistry , vol.21 , pp. 38-43
    • Kato, S.1    Shimamoto, N.2    Utiyama, H.3
  • 119
    • 0027049568 scopus 로고
    • Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation
    • Schultz D.A., Schmid F.X., Baldwin R.L. Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci. 1:1992;917-924.
    • (1992) Protein Sci. , vol.1 , pp. 917-924
    • Schultz, D.A.1    Schmid, F.X.2    Baldwin, R.L.3
  • 120
    • 0029810821 scopus 로고    scopus 로고
    • Nature of the unfolded state of ribonuclease A: Effect of cis-trans X-Pro peptide bond isomerization
    • Houry W.A., Scheraga H.A. Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization. Biochemistry. 35:1996;11719-11733.
    • (1996) Biochemistry , vol.35 , pp. 11719-11733
    • Houry, W.A.1    Scheraga, H.A.2
  • 121
    • 0030919180 scopus 로고    scopus 로고
    • Kinetic folding and cis/trans prolyl isomerization of staphylococcal nuclease. A study by stopped-flow absorption, stopped-flow circular dichroism, and molecular dynamics simulations
    • Ikura T., Tsurupa G.P., Kuwajima K. Kinetic folding and cis/trans prolyl isomerization of staphylococcal nuclease. A study by stopped-flow absorption, stopped-flow circular dichroism, and molecular dynamics simulations. Biochemistry. 36:1997;6529-6538.
    • (1997) Biochemistry , vol.36 , pp. 6529-6538
    • Ikura, T.1    Tsurupa, G.P.2    Kuwajima, K.3
  • 122
    • 0032552972 scopus 로고    scopus 로고
    • The role of ligand binding in the kinetic folding mechanism of human p21 (H-ras) protein
    • Zhang J., Matthews C.R. The role of ligand binding in the kinetic folding mechanism of human p21 (H-ras) protein. Biochemistry. 37:1998;14891-14899.
    • (1998) Biochemistry , vol.37 , pp. 14891-14899
    • Zhang, J.1    Matthews, C.R.2
  • 123
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elove G.A., Bhuyan A.K., Roder H. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry. 33:1994;6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elove, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 124
    • 0021659707 scopus 로고
    • Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor
    • Creighton T.E., Goldenberg D.P. Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 179:1984;497-526.
    • (1984) J. Mol. Biol. , vol.179 , pp. 497-526
    • Creighton, T.E.1    Goldenberg, D.P.2
  • 127
    • 0033554860 scopus 로고    scopus 로고
    • Folding and assembly of dimeric human glutathione transferase A1-1
    • Wallace L.A., Dirr H.W. Folding and assembly of dimeric human glutathione transferase A1-1. Biochemistry. 38:1999;16686-16694.
    • (1999) Biochemistry , vol.38 , pp. 16686-16694
    • Wallace, L.A.1    Dirr, H.W.2
  • 128
    • 0034716941 scopus 로고    scopus 로고
    • The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH
    • Lu H., Booth P.J. The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH. J. Mol. Biol. 299:2000;233-243.
    • (2000) J. Mol. Biol. , vol.299 , pp. 233-243
    • Lu, H.1    Booth, P.J.2


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