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Volumn 31, Issue 11, 1998, Pages 755-763

Protein Folding Triggered by Electron Transfer

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EID: 0000122609     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar970078t     Document Type: Article
Times cited : (111)

References (76)
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to Pathways to Funnels
    • Dill, K. A.; Chan, H. S. From Levinthal to Pathways to Funnels. Nat. Struct. Biol. 1997, 4, 10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 3
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical Studies of Protein-Folding Thermodynamics and Kinetics
    • Shakhnovich, E. I. Theoretical Studies of Protein-Folding Thermodynamics and Kinetics. Curr. Opin. Struct. Biol. 1997, 7, 29-40.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 4
    • 0031465967 scopus 로고    scopus 로고
    • "New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding Simulations
    • Lazaridis, T.; Karplus, M. "New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding Simulations. Science 1997, 278, 1928-1931.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 6
    • 0037889340 scopus 로고
    • Picosecond Fluorescence Studies of Polypeptide Dynamics: Fluorescence Anisotropies and Lifetimes
    • Chen, L. X.-Q.; Petrich, J. W.; Fleming, G. R.; Perico, A. Picosecond Fluorescence Studies of Polypeptide Dynamics: Fluorescence Anisotropies and Lifetimes. Chem. Phys. Lett. 1987, 139, 55-61.
    • (1987) Chem. Phys. Lett. , vol.139 , pp. 55-61
    • Chen, L.X.-Q.1    Petrich, J.W.2    Fleming, G.R.3    Perico, A.4
  • 8
    • 0027370063 scopus 로고
    • Characterization of a Folding Intermediate of Apoplastocyanin Trapped by Proline Isomerization
    • Koide, S.; Dyson, H. J.; Wright, P. E. Characterization of a Folding Intermediate of Apoplastocyanin Trapped by Proline Isomerization. Biochemistry 1993, 32, 12299-12310.
    • (1993) Biochemistry , vol.32 , pp. 12299-12310
    • Koide, S.1    Dyson, H.J.2    Wright, P.E.3
  • 9
    • 0028327236 scopus 로고
    • Protein Folding Dynamics: The Diffusion-Collision Model and Experimental Data
    • Karplus, M.; Weaver, D. L. Protein Folding Dynamics: The Diffusion-Collision Model and Experimental Data. Protein Sci. 1994, 3, 650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 10
    • 0028882223 scopus 로고
    • Simple Model of Protein Folding Kinetics
    • Zwanzig, R. Simple Model of Protein Folding Kinetics. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 9801-9804.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 12
    • 0028352044 scopus 로고
    • Kinetic Mechanism of Cytochrome c Folding: Involvement of the Heme and its Ligands
    • Elöve, G.; Bhuyan, A. K.; Roder, H. Kinetic Mechanism of Cytochrome c Folding: Involvement of the Heme and its Ligands. Biochemistry 1994, 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.1    Bhuyan, A.K.2    Roder, H.3
  • 14
    • 0028387381 scopus 로고
    • Finding Intermediates in Protein Folding
    • Baldwin, R. L. Finding Intermediates in Protein Folding. BioEssays 1994, 16, 207-210.
    • (1994) BioEssays , vol.16 , pp. 207-210
    • Baldwin, R.L.1
  • 15
    • 0028958601 scopus 로고
    • Characterizing Transition States in Protein Folding: An Essential Step in the Puzzle
    • Fersht, A. R. Characterizing Transition States in Protein Folding: an Essential Step in the Puzzle. Curr. Opin. Struct. Biol. 1995, 5, 79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 16
    • 0029124248 scopus 로고
    • Molten Globule and Protein Folding
    • Ptitsyn, O. B. Molten Globule and Protein Folding. Adv. Protein Chem. 1995, 47, 83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 17
    • 0026653655 scopus 로고
    • Protein Folding Studies Using Hydrogen-Exchange Labeling and Two-Dimensional NMR
    • Englander, S. W.; Mayne, L. Protein Folding Studies Using Hydrogen-Exchange Labeling and Two-Dimensional NMR. Annu. Rev. Biophys. Biomol. Struct. 1992, 21, 243-265.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 18
    • 0030272670 scopus 로고    scopus 로고
    • Time-Resolved Biophysical Methods in the Study of Protein Folding
    • Plaxco, K.; Dobson, C. M. Time-Resolved Biophysical Methods in the Study of Protein Folding. Curr. Opin. Struct. Biol. 1996, 6, 630-636.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 630-636
    • Plaxco, K.1    Dobson, C.M.2
  • 19
    • 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. Rapid Formation of Secondary Structure Framework in Protein Folding Studied by Stopped-Flow Circular Dichroism. FEBS Lett. 1987, 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
  • 20
    • 0028882589 scopus 로고
    • P22 Arc Repressor: Transition State Properties Inferred from Mutational Effects on the Rates of Protein Unfolding and Refolding
    • Milla, M. E.; Brown, B. M.; Waldburger, C. D.; Sauer, R. T. P22 Arc Repressor: Transition State Properties Inferred from Mutational Effects on the Rates of Protein Unfolding and Refolding. Biochemistry 1995, 34, 13914-13919.
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 21
    • 0028788480 scopus 로고
    • Evidence for a Two-State Transition in the Folding Process of the Activation Domain of Human Procarboxypeptidase A2
    • Villegas, V.; Azuaga, A.; Catasús, L.; Reverter, D.; Mateo, P. L.; Avilés, F. X.; Serrano, L. Evidence for a Two-State Transition in the Folding Process of the Activation Domain of Human Procarboxypeptidase A2. Biochemistry 1995, 34, 15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasús, L.3    Reverter, D.4    Mateo, P.L.5    Avilés, F.X.6    Serrano, L.7
  • 22
    • 0028232822 scopus 로고
    • The Refolding of Human Lysozyme: A Comparison with the Structurally Homologous Hen Lysozyme
    • Hooke, S. D.; Radford, S. E.; Dobson, C. M. The Refolding of Human Lysozyme: A Comparison with the Structurally Homologous Hen Lysozyme. Biochemistry 1994, 33, 5867-5876.
    • (1994) Biochemistry , vol.33 , pp. 5867-5876
    • Hooke, S.D.1    Radford, S.E.2    Dobson, C.M.3
  • 23
    • 0029003514 scopus 로고
    • Folding of a Four-Helix Bundle: Studies of Acyl-Coenzyme a Binding Protein
    • Kragelund, B. B.; Robinson, C. V.; Knudsen, J.; Dobson, C. M.; Poulsen, F. M. Folding of a Four-Helix Bundle: Studies of Acyl-Coenzyme A Binding Protein. Biochemistry 1995, 34, 7217-7224.
    • (1995) Biochemistry , vol.34 , pp. 7217-7224
    • Kragelund, B.B.1    Robinson, C.V.2    Knudsen, J.3    Dobson, C.M.4    Poulsen, F.M.5
  • 24
    • 0028140319 scopus 로고
    • Hydrogen Exchange Rates and Protein Folding
    • Woodward, C. K. Hydrogen Exchange Rates and Protein Folding. Curr. Opin. Struct. Biol. 1994, 4, 112-116.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 112-116
    • Woodward, C.K.1
  • 25
    • 0029763434 scopus 로고    scopus 로고
    • Rapid Refolding of a Proline-Rich All-Beta-Sheet Fibronectin Type III Module
    • Plaxco, K. W.; Claus, S.; Campbell, I. D.; Dobson, C. M. Rapid Refolding of a Proline-Rich All-Beta-Sheet Fibronectin Type III Module. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 10703-10706.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10703-10706
    • Plaxco, K.W.1    Claus, S.2    Campbell, I.D.3    Dobson, C.M.4
  • 26
    • 0029643523 scopus 로고
    • Protein Folding Intermediates: Native-State Hydrogen Exchange
    • Bai, Y.; Sosnick, T. R.; Mayne, L.; Englander, S. W. Protein Folding Intermediates: Native-State Hydrogen Exchange. Science 1995, 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 27
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen Exchange: The Modern Legacy of Linderstrøm-Lang
    • Englander, S. W.; Mayne, L.; Bai, Y.; Sosnick, T. R. Hydrogen Exchange: The Modern Legacy of Linderstrøm-Lang. Protein Sci. 1997, 6, 1101-1109.
    • (1997) Protein Sci. , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 28
    • 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. Early Steps in Cytochrome c Folding Probed by Time-Resolved Circular Dichroism and Fluorescence Spectroscopy. Biochemistry 1992, 31, 6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.4
  • 29
    • 0029738416 scopus 로고    scopus 로고
    • Circular Dichroism Evidence for the Presence of Burst-Phase Intermediates on the Conformational Folding Pathway of Ribonuclease A
    • Houry, W. A.; Rothwarf, D. M.; Scheraga, H. A. Circular Dichroism Evidence for the Presence of Burst-Phase Intermediates on the Conformational Folding Pathway of Ribonuclease A. Biochemistry 1996, 35, 10125-10133.
    • (1996) Biochemistry , vol.35 , pp. 10125-10133
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 30
    • 0030348041 scopus 로고    scopus 로고
    • Rapid Formation of a Molten Globule Intermediate in Refolding of α-Lactalbumin
    • Arai, M.; Kuwajima, K. Rapid Formation of a Molten Globule Intermediate in Refolding of α-Lactalbumin. Folding Des. 1996, 1, 275-287.
    • (1996) Folding Des. , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 31
    • 0029598779 scopus 로고
    • Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR Study
    • Yamasaki, K.; Ogasahara, K.; Yutani, K.; Oobatake, M.; Kanaya, S. Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR Study. Biochemistry 1995, 34, 16552-16562.
    • (1995) Biochemistry , vol.34 , pp. 16552-16562
    • Yamasaki, K.1    Ogasahara, K.2    Yutani, K.3    Oobatake, M.4    Kanaya, S.5
  • 32
    • 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. Local and Global Dynamics during the Folding of Escherichia coli Dihydrofolate Reductase by Time-Resolved Fluorescence Spectroscopy. Biochemistry 1995, 34, 1867-1877.
    • (1995) Biochemistry , vol.34 , pp. 1867-1877
    • Jones, B.E.1    Beechem, J.M.2    Matthews, C.R.3
  • 34
    • 85033930038 scopus 로고    scopus 로고
    • Submillisecond Processes in Protein Folding Studied by Ultrarapid Mixing and Continuous Flow
    • Chan, C. K.; Eaton, W. A.; Hofrichter, J. Submillisecond Processes in Protein Folding Studied by Ultrarapid Mixing and Continuous Flow. Biophys. J. 1997, 72, 383.
    • (1997) Biophys. J. , vol.72 , pp. 383
    • Chan, C.K.1    Eaton, W.A.2    Hofrichter, J.3
  • 37
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for Barrier-Limited Protein-Folding Kinetics on the Microsecond Time-Scale
    • Shastry, M. C. R.; Roder, H. Evidence for Barrier-Limited Protein-Folding Kinetics on the Microsecond Time-Scale. Nat. Struct. Biol. 1998, 5, 385-392.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 40
    • 0029973119 scopus 로고    scopus 로고
    • Direct Observation of Fast Protein Folding: The Initial Collapse of Apomyoglobin
    • Ballew, R. M.; Sabelko, J.; Gruebele, M. Direct Observation of Fast Protein Folding: The Initial Collapse of Apomyoglobin. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 5759-5764.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 41
    • 0000476554 scopus 로고
    • Fast Events in Protein Folding -Laser T-jump Time-Resolved Infrared Study of the Ribonuclease-A S-peptide
    • Woodruff, W. H.; Dyer, R. B.; Callender, R. H.; Paige, K.; Causgrove, T. Fast Events in Protein Folding -Laser T-jump Time-Resolved Infrared Study of the Ribonuclease-A S-peptide. Biophys. J. 1994, 66, A397.
    • (1994) Biophys. J. , vol.66
    • Woodruff, W.H.1    Dyer, R.B.2    Callender, R.H.3    Paige, K.4    Causgrove, T.5
  • 43
    • 0038502170 scopus 로고    scopus 로고
    • Folding Dynamics and Mechanism of Beta-Hairpin Formation
    • Munoz, V.; Thompson, P. A.; Hofrichter, J.; Eaton, W. A. Folding Dynamics and Mechanism of Beta-Hairpin Formation. Nature 1997, 390, 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 44
    • 0030789351 scopus 로고    scopus 로고
    • Laser Temperature-Jump Study of the Helix ⇌ Coil Kinetics of an Alanine Peptide Interpreted with a Kinetic Zipper Model
    • Thompson, P. A.; Eaton, W. A.; Hofrichter, J. Laser Temperature-Jump Study of the Helix ⇌ Coil Kinetics of an Alanine Peptide Interpreted with a Kinetic Zipper Model. Biochemistry 1997, 36, 9200-9210.
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 45
    • 0030584652 scopus 로고    scopus 로고
    • Protein Folding Triggered by Electron Transfer
    • Pascher, T.; Chesick, J. P.; Winkler, J. R.; Gray, H. B. Protein Folding Triggered by Electron Transfer. Science 1996, 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
  • 46
    • 0023044641 scopus 로고
    • Control of the Redox Potential of Cytochrome c and Microscopic Dielectric Effects in Proteins
    • Churg, A. K.; Warshel, A. Control of the Redox Potential of Cytochrome c and Microscopic Dielectric Effects in Proteins. Biochemistry 1986, 25, 1675-1681.
    • (1986) Biochemistry , vol.25 , pp. 1675-1681
    • Churg, A.K.1    Warshel, A.2
  • 47
    • 2642646038 scopus 로고
    • Electrochemical Probes of Protein Folding
    • Bixler, J.; Bakker, G.; McLendon, G. Electrochemical Probes of Protein Folding. J. Am. Chem. Soc. 1992, 114, 6938-6939.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6938-6939
    • Bixler, J.1    Bakker, G.2    McLendon, G.3
  • 48
    • 0026545583 scopus 로고
    • Folding Kinetics of T4 Lysozyme and Nine Mutants at 12 °C
    • Chen, B.-L.; Baase, W. A.; Nicholson, H.; Schellman, J. A. Folding Kinetics of T4 Lysozyme and Nine Mutants at 12 °C Biochemistry 1992, 31, 1464-1476.
    • (1992) Biochemistry , vol.31 , pp. 1464-1476
    • Chen, B.-L.1    Baase, W.A.2    Nicholson, H.3    Schellman, J.A.4
  • 50
    • 0028960492 scopus 로고
    • How Valid are Denaturant-Induced Free Energy Measurements? Level of Confidence to Common Assumptions over an Extended Range of Ribonuclease a Stability
    • Yao, M.; Bolen, D. W. How Valid are Denaturant-Induced Free Energy Measurements? Level of Confidence to Common Assumptions over an Extended Range of Ribonuclease A Stability. Biochemistry 1995, 34, 3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 53
    • 84940923561 scopus 로고    scopus 로고
    • Spectroscopic Studies of Ferrocytochrome c Folding
    • Solomon, E. I., Hodgson, K. O., Eds.; American Chemical Society: Washington, DC
    • Mines, G. A.; Winkler, J. R.; Gray, H. B. Spectroscopic Studies of Ferrocytochrome c Folding. In Spectroscopic Methods in Bioinorganic Chemistry, Solomon, E. I., Hodgson, K. O., Eds.; American Chemical Society: Washington, DC, 1998.
    • (1998) Spectroscopic Methods in Bioinorganic Chemistry
    • Mines, G.A.1    Winkler, J.R.2    Gray, H.B.3
  • 56
    • 85033920714 scopus 로고    scopus 로고
    • Role of Ligand Substitution in Ferrocytochrome c Folding
    • submitted for publication
    • Telford, J. R.; Tezcan, F. A.; Gray, H. B.; Winkler, J. R. Role of Ligand Substitution in Ferrocytochrome c Folding. Biochemistry, submitted for publication.
    • Biochemistry
    • Telford, J.R.1    Tezcan, F.A.2    Gray, H.B.3    Winkler, J.R.4
  • 57
    • 0027489837 scopus 로고
    • Immediate Reduction of Cytochrome c by Photoexcited NADH. Reaction Mechanism as Revealed by Flow Flash and Rapid-Scan Studies
    • Orii, Y. Immediate Reduction of Cytochrome c by Photoexcited NADH. Reaction Mechanism as Revealed by Flow Flash and Rapid-Scan Studies. Biochemistry 1993, 32, 11910-11914.
    • (1993) Biochemistry , vol.32 , pp. 11910-11914
    • Orii, Y.1
  • 58
    • 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. 1996, 24, 413-426.
    • (1996) Proteins: Struct., Funct., Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 60
    • 0029967474 scopus 로고    scopus 로고
    • Side Chain Packing of the N- and C-Terminal Helices Plays a Critical Role in the Kinetics of Cytochrome c Folding
    • Colón, W.; Elöve, G. A.; Wakem, L. P.; Sherman, F.; Roder, H. Side Chain Packing of the N- and C-Terminal Helices Plays a Critical Role in the Kinetics of Cytochrome c Folding. Biochemistry 1996, 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
  • 61
    • 0030897736 scopus 로고    scopus 로고
    • Fast Folding of Cytochrome c
    • Pierce, M. M.; Nall, B. T. Fast Folding of Cytochrome c. Protein Sci. 1997, 6, 618-627.
    • (1997) Protein Sci. , vol.6 , pp. 618-627
    • Pierce, M.M.1    Nall, B.T.2
  • 62
    • 0031007307 scopus 로고    scopus 로고
    • Cytochrome c Folding Kinetics Studied by Time-Resolved Electrospray Ionization Mass Spectrometry
    • Konermann, L.; Collings, B. A.; Douglas, D. J. Cytochrome c Folding Kinetics Studied by Time-Resolved Electrospray Ionization Mass Spectrometry. Biochemistry 1997, 36, 5554-5559.
    • (1997) Biochemistry , vol.36 , pp. 5554-5559
    • Konermann, L.1    Collings, B.A.2    Douglas, D.J.3
  • 63
    • 0015526732 scopus 로고
    • Participation of the Protein Ligands in the Folding of Cytochrome c
    • Babul, J.; Stellwagen, E. Participation of the Protein Ligands in the Folding of Cytochrome c. Biochemistry 1972, 11, 1195-1200.
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 64
    • 0025832142 scopus 로고
    • Effective Concentrations of Amino Acid Side Chains in an Unfolded Protein
    • Muthukrishnan, K.; Nall, B. T. Effective Concentrations of Amino Acid Side Chains in an Unfolded Protein. Biochemistry 1991, 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nall, B.T.2
  • 65
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the Predominant Non-Native Histidine Ligand in Unfolded Cytochrome c
    • Colón, W.; Wakem, L. P.; Sherman, F.; Roder, H. Identification of the Predominant Non-Native Histidine Ligand in Unfolded Cytochrome c. Biochemistry 1997, 36, 12535-12541.
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 66
    • 0031584267 scopus 로고    scopus 로고
    • A Histidine Variant of Yeast Iso-1-Cytochrome c that Strongly Affects the Energetics of the Denatured State
    • Godbole, S.; Bowler, B. E. A Histidine Variant of Yeast Iso-1-Cytochrome c that Strongly Affects the Energetics of the Denatured State. J. Mol. Biol. 1997, 268, 816-821.
    • (1997) J. Mol. Biol. , vol.268 , pp. 816-821
    • Godbole, S.1    Bowler, B.E.2
  • 67
    • 0029802355 scopus 로고    scopus 로고
    • Optical Triggers of Protein Folding
    • Chan, C. K.; Hofrichter, J.; Eaton, W. A. Optical Triggers of Protein Folding. Science 1996, 274, 628-629.
    • (1996) Science , vol.274 , pp. 628-629
    • Chan, C.K.1    Hofrichter, J.2    Eaton, W.A.3
  • 68
    • 0031095826 scopus 로고    scopus 로고
    • Rate of Intrachain Diffusion of Unfolded Cytochrome c
    • Hagen, S. J.; Hofrichter, J.; Eaton, W. A. Rate of Intrachain Diffusion of Unfolded Cytochrome c. J. Phys. Chem. B 1997, 101, 2352-2365.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 2352-2365
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 69
    • 0009525454 scopus 로고    scopus 로고
    • Optical Triggers of Protein Folding - Response
    • Winkler, J. R.; Gray, H. B. Optical Triggers Of Protein Folding - Response. Science 1996, 274, 629.
    • (1996) Science , vol.274 , pp. 629
    • Winkler, J.R.1    Gray, H.B.2
  • 70
    • 0025936148 scopus 로고
    • α-Acetyl Microperoxidase-8 with Hydrogen Peroxide: Models for Compounds 0, I and II of Horseradish Peroxidase
    • α-Acetyl Microperoxidase-8 with Hydrogen Peroxide: Models for Compounds 0, I and II of Horseradish Peroxidase. Biochem. Biophys. Res. Commun. 1991, 179, 1320-1324.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1320-1324
    • Wang, J.-S.1    Baek, H.K.2    Van Wart, H.E.3
  • 71
    • 85033909154 scopus 로고    scopus 로고
    • Effects of Ligation and Folding on Reduction Potentials of Heme Proteins
    • submitted for publication
    • Tezcan, F. A.; Winkler, J. R.; Gray, H. B. Effects of Ligation and Folding on Reduction Potentials of Heme Proteins. J. Am. Chem. Soc., submitted for publication.
    • J. Am. Chem. Soc.
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 74
    • 0021280149 scopus 로고
    • 562, Complex from Cells in the Early Exponential Phase of Aerobic Growth
    • 562, Complex from Cells in the Early Exponential Phase of Aerobic Growth. J. Biol. Chem. 1984, 259, 3368-3374.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3368-3374
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 75
    • 0026075970 scopus 로고
    • 562 from Escherichia coli
    • 562 from Escherichia coli. Biochemistry 1991, 30, 10012-10018.
    • (1991) Biochemistry , vol.30 , pp. 10012-10018
    • Fisher, M.T.1
  • 76
    • 0029952910 scopus 로고    scopus 로고
    • Symmetry and the Energy Landscapes of Biomolecules
    • Wolynes, P. G. Symmetry and the Energy Landscapes of Biomolecules. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 14249-14255.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14249-14255
    • Wolynes, P.G.1


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