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Volumn 1, Issue , 2008, Pages 377-410

Kinetic Mechanisms in Protein Folding

Author keywords

Activation; Domains; Equilibrium; Isomerization; Kinetic mechanisms

Indexed keywords


EID: 84888350458     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch12a     Document Type: Chapter
Times cited : (13)

References (83)
  • 1
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states
    • J
    • Sánchez, I. E. & Kiefhaber, T. (2003). Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states. J. Mol. Biol. 327, 867-884.
    • (2003) Mol. Biol. , vol.327 , pp. 867-884
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 2
    • 0029173864 scopus 로고
    • Protein folding kinetics
    • Protein Stability and Folding Protocols (Shirley, B. A., ed.), Humana Press, Totowa, NJ
    • Kiefhaber, T. (1995). Protein folding kinetics. In Methods in Molecular Biology, Vol. 40: Protein Stability and Folding Protocols (Shirley, B. A., ed.), pp. 313-341. Humana Press, Totowa, NJ.
    • (1995) Methods in Molecular Biology , vol.40 , pp. 313-341
    • Kiefhaber, T.1
  • 3
    • 0002203625 scopus 로고    scopus 로고
    • Kinetic models in protein folding
    • In Protein Folding: Frontiers in Molecular Biology 2nd edn (Pain, R., ed.), Oxford University Press, Oxford
    • Bieri, O. & Kiefhaber, T. (2000). Kinetic models in protein folding. In Protein Folding: Frontiers in Molecular Biology 2nd edn (Pain, R., ed.), pp. 34-64. Oxford University Press, Oxford.
    • (2000) , pp. 34-64
    • Bieri, O.1    Kiefhaber, T.2
  • 4
    • 85012750408 scopus 로고
    • Kinetic characterization of complex reaction systems
    • (Bamford, C. H. & Tipper, C. F. H., eds), 7 vols. Elsevier Publishing Company, Amsterdam
    • Szabo, Z. G. (1969). Kinetic characterization of complex reaction systems. In Comprehensive Chemical Kinetics (Bamford, C. H. & Tipper, C. F. H., eds), Vol. 2, pp. 1-80. 7 vols. Elsevier Publishing Company, Amsterdam.
    • (1969) Comprehensive Chemical Kinetics , vol.2 , pp. 1-80
    • Szabo, Z.G.1
  • 5
    • 0003960770 scopus 로고
    • Kinetics and Mechanisms
    • John Wiley & Sons, New York
    • Moore, J. W. & Pearson, R. G. (1981). Kinetics and Mechanisms. John Wiley & Sons, New York.
    • (1981)
    • Moore, J.W.1    Pearson, R.G.2
  • 6
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E. (1998). How do small single-domain proteins fold? Folding Design 3, R81-R91.
    • (1998) Folding Design , vol.3
    • Jackson, S.E.1
  • 7
    • 2142746284 scopus 로고
    • The activated complex in chemical reactions
    • Eyring, H. (1935). The activated complex in chemical reactions. J. Chem. Phys. 3, 107-115.
    • (1935) J. Chem. Phys. , vol.3 , pp. 107-115
    • Eyring, H.1
  • 8
    • 37049147605 scopus 로고
    • Some applications of the transition state method to the calculation of reaction velocities, especially in solution
    • Evans, M. G. & Polanyi, M. (1935). Some applications of the transition state method to the calculation of reaction velocities, especially in solution. Trans. Faraday Soc. 31, 875-885.
    • (1935) Trans. Faraday Soc. , vol.31 , pp. 875-885
    • Evans, M.G.1    Polanyi, M.2
  • 9
    • 0043237588 scopus 로고    scopus 로고
    • Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding
    • Krieger, F., Fierz, B., Bieri, O., Drewello, M. & Kiefhaber, T. (2003). Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding. J. Mol. Biol. 332, 265-274.
    • (2003) J. Mol. Biol. , vol.332 , pp. 265-274
    • Krieger, F.1    Fierz, B.2    Bieri, O.3    Drewello, M.4    Kiefhaber, T.5
  • 10
    • 0016292941 scopus 로고
    • Urea and guanidine-hydrochloride denaturation of ribonuclease, lysozyme, alpha-chyomtrypsinn and beta-lactoglobulin
    • Greene, R. F. J. & Pace, C. N. (1974). Urea and guanidine-hydrochloride denaturation of ribonuclease, lysozyme, alpha-chyomtrypsinn and beta-lactoglobulin. J. Biol. Chem. 249, 5388-5393.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.J.1    Pace, C.N.2
  • 11
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alphachymotrypsin using different denaturants
    • Santoro, M. M. & Bolen, D. W. (1988). Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alphachymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 12
    • 0014718113 scopus 로고
    • Protein Denaturation. Part C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970). Protein Denaturation. Part C. Theoretical models for the mechanism of denaturation. Adv. Prot. Chem. 24, 1-95.
    • (1970) Adv. Prot. Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 13
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c
    • Ikai, A., Fish, W. W. & Tanford, C. (1973). Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c. J. Mol. Biol. 73, 165-184.
    • (1973) J. Mol. Biol. , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 14
    • 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. Methods Enzymol. 154, 498-511.
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 15
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 16
    • 0000288714 scopus 로고
    • Parameters for the description of transition states
    • Leffler, J. E. (1953). Parameters for the description of transition states. Science 117, 340-341.
    • (1953) Science , vol.117 , pp. 340-341
    • Leffler, J.E.1
  • 17
    • 0003558028 scopus 로고
    • Rates and Equilibria of Organic Reactions
    • Dover, New York
    • Leffler, J. E. & Grunwald, E. (1963). Rates and Equilibria of Organic Reactions. Dover, New York.
    • (1963)
    • Leffler, J.E.1    Grunwald, E.2
  • 18
    • 0003408336 scopus 로고
    • Catalysis in Chemistry and Enzymology
    • McGraw-Hill, New York
    • Jencks, W. P. (1969). Catalysis in Chemistry and Enzymology. McGraw-Hill, New York.
    • (1969)
    • Jencks, W.P.1
  • 19
    • 0037438623 scopus 로고    scopus 로고
    • Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
    • Sánchez, I. E. & Kiefhaber, T. (2003). Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding. Biophys. Chem. 100, 397-407.
    • (2003) Biophys. Chem. , vol.100 , pp. 397-407
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 20
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins. I. Mathematical Analysis
    • Ikai, A. & Tanford, C. (1973). Kinetics of unfolding and refolding of proteins. I. Mathematical Analysis. J. Mol. Biol. 73, 145-163.
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2
  • 21
    • 0015918873 scopus 로고
    • Kinetics of unfolding and refolding of proteins. III. Results for lysozyme
    • Tanford, C., Aune, K. C. & Ikai, A. (1973). Kinetics of unfolding and refolding of proteins. III. Results for lysozyme. J. Mol. Biol. 73, 185-197.
    • (1973) J. Mol. Biol. , vol.73 , pp. 185-197
    • Tanford, C.1    Aune, K.C.2    Ikai, A.3
  • 22
    • 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
  • 23
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model for 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 for protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat. Struct. Biol. 3, 193-205.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 24
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models
    • Kiefhaber, T., Kohler, H. H. & Schmid, F. X. (1992). Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. J. Mol. Biol. 224, 217-229.
    • (1992) J. Mol. Biol. , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Kohler, H.H.2    Schmid, F.X.3
  • 25
    • 0026538017 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1
    • Kiefhaber, T. & Schmid, F. X. (1992). Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1. J. Mol. Biol. 224, 231-240.
    • (1992) J. Mol. Biol. , vol.224 , pp. 231-240
    • Kiefhaber, T.1    Schmid, F.X.2
  • 27
    • 0032847748 scopus 로고    scopus 로고
    • Elementary steps in protein folding
    • Bieri, O. & Kiefhaber, T. (1999). Elementary steps in protein folding. Biol. Chem. 380, 923-929.
    • (1999) Biol. Chem. , vol.380 , pp. 923-929
    • Bieri, O.1    Kiefhaber, T.2
  • 29
    • 0015715985 scopus 로고
    • Both the fast and slow folding reactions of ribonuclease A yield native enzyme
    • Garel, J. R. & Baldwin, R. L. (1973). Both the fast and slow folding reactions of ribonuclease A yield native enzyme. Proc. Natl Acad. Sci. U.S.A. 70, 3347-3351.
    • (1973) Proc. Natl Acad. Sci. U.S.A. , vol.70 , pp. 3347-3351
    • Garel, J.R.1    Baldwin, R.L.2
  • 30
    • 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. (1975). Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 31
    • 0025311245 scopus 로고
    • Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding
    • Kiefhaber, T., Grunert, H. P., Hahn, U. & Schmid, F. X. (1990). Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry 29, 6475-6480.
    • (1990) Biochemistry , vol.29 , pp. 6475-6480
    • Kiefhaber, T.1    Grunert, H.P.2    Hahn, U.3    Schmid, F.X.4
  • 32
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang, K., Schmid, F. X. & Fischer, G. (1987). Catalysis of protein folding by prolyl isomerase. Nature 329, 268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 34
    • 0000247412 scopus 로고    scopus 로고
    • Proline isomerization and its catalysis in protein folding
    • (Pain, R., ed.). Oxford University Press, Oxford
    • Balbach, J. & Schmid, F. X. (2000). Proline isomerization and its catalysis in protein folding. In Protein Folding: Frontiers in Molecular Biology (Pain, R., ed.). Oxford University Press, Oxford.
    • (2000) Protein Folding: Frontiers in Molecular Biology
    • Balbach, J.1    Schmid, F.X.2
  • 35
    • 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. (1990). Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29, 3053-3061.
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 36
    • 0025195732 scopus 로고
    • Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions
    • Kiefhaber, T., Quaas, R., Hahn, U. & Schmid, F. X. (1990). Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry 29, 3061-3070.
    • (1990) Biochemistry , vol.29 , pp. 3061-3070
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 37
    • 0028870213 scopus 로고
    • Non-prolyl cis/trans peptide bond isomerization as a ratedeterminig step in protein unfolding and refolding
    • Odefey, C., Mayr, L. & Schmid, F. X. (1995). Non-prolyl cis/trans peptide bond isomerization as a ratedeterminig step in protein unfolding and refolding. J. Mol. Biol. 245, 69-78.
    • (1995) J. Mol. Biol. , vol.245 , pp. 69-78
    • Odefey, C.1    Mayr, L.2    Schmid, F.X.3
  • 40
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Colon, 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
    • Colon, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 42
    • 0031952599 scopus 로고    scopus 로고
    • Folding intermediates in cytochrome c
    • Yeh, S.-R. & Rousseau, D. L. (1998). Folding intermediates in cytochrome c. Nat. Struct. Biol. 5, 222-228.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 222-228
    • Yeh, S.-R.1    Rousseau, D.L.2
  • 43
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in lysozyme folding with time-resolved small angle X-ray scattering
    • Segel, D., Bachmann, A., Hofrichter, J., Hodgson, K., Doniach, S. & Kiefhaber, T. (1999). Characterization of transient intermediates in lysozyme folding with time-resolved small angle X-ray scattering. J. Mol. Biol. 288, 489-500.
    • (1999) J. Mol. Biol. , vol.288 , pp. 489-500
    • Segel, D.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.4    Doniach, S.5    Kiefhaber, T.6
  • 44
    • 0037007487 scopus 로고    scopus 로고
    • Test for cooperativity in the early kinetic intermediate in lysozyme folding
    • Bachmann, A. & Kiefhaber, T. (2002). Test for cooperativity in the early kinetic intermediate in lysozyme folding. Biophys. Chem. 96, 141-151.
    • (2002) Biophys. Chem. , vol.96 , pp. 141-151
    • Bachmann, A.1    Kiefhaber, T.2
  • 45
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 46
    • 0028952169 scopus 로고
    • Bipartite structure of the alactalbumin molten globule
    • Wu, L. C., Peng, Z.-Y. & Kim, P. S. (1995). Bipartite structure of the alactalbumin molten globule. Nat. Struct. Biol. 2, 281-286.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.-Y.2    Kim, P.S.3
  • 47
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the alactalbumin molten globule
    • Wu, L. C. & Kim, P. S. (1998). A specific hydrophobic core in the alactalbumin molten globule. J. Mol. Biol. 280, 175-182.
    • (1998) J. Mol. Biol. , vol.280 , pp. 175-182
    • Wu, L.C.1    Kim, P.S.2
  • 48
    • 0033613115 scopus 로고    scopus 로고
    • The 28-111 disulfide bond contrains the alactalbumin molten globule and weakens its cooperativity of folding
    • Luo, Y. & Baldwin, R. L. (1999). The 28-111 disulfide bond contrains the alactalbumin molten globule and weakens its cooperativity of folding. Proc. Natl Acad. Sci. USA 96, 11283-11287.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11283-11287
    • Luo, Y.1    Baldwin, R.L.2
  • 49
    • 0030694241 scopus 로고    scopus 로고
    • Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • Luo, Y., Kay, M. S. & Baldwin, R. L. (1997). Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations. Nat. Struct. Biol. 4, 925-929.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 925-929
    • Luo, Y.1    Kay, M.S.2    Baldwin, R.L.3
  • 50
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easilty mistaken for folding intermediates
    • Silow, M. & Oliveberg, M. (1997). Transient aggregates in protein folding are easilty 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
  • 51
    • 0021113912 scopus 로고
    • Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates
    • Schmid, F. X. (1983). Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry 22, 4690-4696.
    • (1983) Biochemistry , vol.22 , pp. 4690-4696
    • Schmid, F.X.1
  • 52
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G. & Kiefhaber, T. (1997). Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270, 294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 53
    • 0016180488 scopus 로고
    • The sliding filament model of contraction of striated muscle
    • Hill, T. L. (1974). The sliding filament model of contraction of striated muscle. Progr. Biophys. Mol. Biol. 28, 267-340.
    • (1974) Progr. Biophys. Mol. Biol. , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 54
    • 0003817483 scopus 로고
    • Free Energy Transduction in Biology
    • Academic Press, London
    • Hill, T. L. (1977). Free Energy Transduction in Biology. Academic Press, London.
    • (1977)
    • Hill, T.L.1
  • 55
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: predominance of native intermediates
    • Weismann, J. S. & Kim, P. S. (1991). Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weismann, J.S.1    Kim, P.S.2
  • 56
    • 0026584375 scopus 로고
    • Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate
    • Kiefhaber, T., Grunert, H. P., Hahn, U. & Schmid, F. X. (1992). Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate. Proteins Struct. Funct. Genet. 12, 171-179.
    • (1992) Proteins Struct. Funct. Genet. , vol.12 , pp. 171-179
    • Kiefhaber, T.1    Grunert, H.P.2    Hahn, U.3    Schmid, F.X.4
  • 57
    • 0035895436 scopus 로고    scopus 로고
    • Apparent two-state tendamistat folding is a sequential process along a defined route
    • Bachmann, A. & Kiefhaber, T. (2001). Apparent two-state tendamistat folding is a sequential process along a defined route. J. Mol. Biol. 306, 375-386.
    • (2001) J. Mol. Biol. , vol.306 , pp. 375-386
    • Bachmann, A.1    Kiefhaber, T.2
  • 58
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sánchez, 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
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 59
    • 33847086871 scopus 로고
    • When is an intermediate not an intermediate? Enforced mechanisms of general acidbase catalyzed, carbonation, carbanion, and ligand exchange reactions
    • Jencks, W. P. (1980). When is an intermediate not an intermediate? Enforced mechanisms of general acidbase catalyzed, carbonation, carbanion, and ligand exchange reactions. Acc. Chem. Res. 13, 161-169.
    • (1980) Acc. Chem. Res. , vol.13 , pp. 161-169
    • Jencks, W.P.1
  • 60
    • 0030917229 scopus 로고    scopus 로고
    • Direct measurements of nucleation and growth rates in lysozyme folding
    • Kiefhaber, T., Bachmann, A., Wildegger, G. & Wagner, C. (1997). Direct measurements of nucleation and growth rates in lysozyme folding. Biochemistry 36, 5108-5112.
    • (1997) Biochemistry , vol.36 , pp. 5108-5112
    • Kiefhaber, T.1    Bachmann, A.2    Wildegger, G.3    Wagner, C.4
  • 61
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
    • Walkenhorst, W. F., Green, S. & Roder, H. (1997). Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry 36, 5795-5805.
    • (1997) Biochemistry , vol.36 , pp. 5795-5805
    • Walkenhorst, W.F.1    Green, S.2    Roder, H.3
  • 64
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and alactalbumin
    • Kuwajima, K., Hiraoka, Y., Ikeguchui, M. & Sugai, S. (1985). Comparison of the transient folding intermediates in lysozyme and alactalbumin. Biochemistry 24, 874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchui, M.3    Sugai, S.4
  • 65
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and sidechain far-UV CD during folding of HEWL
    • Chaffotte, A. F., Guillou, Y. & Goldberg, M. E. (1992). Kinetic resolution of peptide bond and sidechain far-UV CD during folding of HEWL. Biochemistry 31, 9694-9702.
    • (1992) Biochemistry , vol.31 , pp. 9694-9702
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 66
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes
    • Itzhaki, L. S., Evans, P. A., Dobson, C. M. & Radford, S. E. (1994). Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 33, 5212-5220.
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 67
    • 0026731991 scopus 로고
    • Hydrogen exchange in native and denatured states of hen egg-white lysozyme
    • Radford, S. E., Buck, M., Topping, K. D., Dobson, C. M. & Evans, P. A. (1992). Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins 14, 237-248.
    • (1992) Proteins , vol.14 , pp. 237-248
    • Radford, S.E.1    Buck, M.2    Topping, K.D.3    Dobson, C.M.4    Evans, P.A.5
  • 68
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectroscopy
    • Miranker, A. D., Robinson, C. V., Radford, S. E., Aplin, R. T. & Dobson, C. M. (1993). Detection of transient protein folding populations by mass spectroscopy. Science 262, 896-900.
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.D.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 72
    • 0029904097 scopus 로고    scopus 로고
    • Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme
    • Rothwarf, D. M. & Scheraga, H. A. (1996). Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry 35, 13797-13807.
    • (1996) Biochemistry , vol.35 , pp. 13797-13807
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 73
    • 0035919775 scopus 로고    scopus 로고
    • Origin of apparent fast and nonexponential kinetics of lysozyme folding measured in pulse labeling experiments
    • Bieri, O. & Kiefhaber, T. (2001). Origin of apparent fast and nonexponential kinetics of lysozyme folding measured in pulse labeling experiments. J. Mol. Biol. 310, 919-935.
    • (2001) J. Mol. Biol. , vol.310 , pp. 919-935
    • Bieri, O.1    Kiefhaber, T.2
  • 75
    • 0033592403 scopus 로고    scopus 로고
    • A salt-induced intermediate is on a new parallel pathway of lysozyme folding
    • Bieri, O., Wildegger, G., Bachmann, A., Wagner, C. & Kiefhaber, T. (1999). A salt-induced intermediate is on a new parallel pathway of lysozyme folding. Biochemistry 38, 12460-12470.
    • (1999) Biochemistry , vol.38 , pp. 12460-12470
    • Bieri, O.1    Wildegger, G.2    Bachmann, A.3    Wagner, C.4    Kiefhaber, T.5
  • 76
    • 80355140158 scopus 로고
    • Über das Dellmann'sche Elektrometer
    • Kohlrausch, R. (1847). Über das Dellmann'sche Elektrometer. Ann. Phys. Chem. 11, 353-405.
    • (1847) Ann. Phys. Chem. , vol.11 , pp. 353-405
    • Kohlrausch, R.1
  • 78
    • 0001081429 scopus 로고
    • Kinetics of protein folding: The folding dynamics of globally connected rough energy landscapes with biases
    • Saven, J. G., Wang, J. & Wolynes, P. G. (1994). Kinetics of protein folding: The folding dynamics of globally connected rough energy landscapes with biases. J. Chem. Phys. 101, 11037-11043.
    • (1994) J. Chem. Phys. , vol.101 , pp. 11037-11043
    • Saven, J.G.1    Wang, J.2    Wolynes, P.G.3
  • 79
    • 0000620198 scopus 로고    scopus 로고
    • Non-Arrhenius behavior in the realaxation of model proteins
    • Skorobogatiy, M., Guo, H. & Zuckermann, M. (1998). Non-Arrhenius behavior in the realaxation of model proteins. J. Chem. Phys. 109, 2528-2535.
    • (1998) J. Chem. Phys. , vol.109 , pp. 2528-2535
    • Skorobogatiy, M.1    Guo, H.2    Zuckermann, M.3
  • 81
    • 0029647450 scopus 로고
    • Protein kinetics in a glass at room temperature
    • Hagen, S. J., Hofrichter, J. & Eaton, W. A. (1995). Protein kinetics in a glass at room temperature. Science 269, 959-962.
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 82
    • 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
  • 83
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. & Gruebele, M. (2003). Folding at the speed limit. Nature 423, 193-197.
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2


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