메뉴 건너뛰기




Volumn 75, Issue 1, 1998, Pages 428-434

Protein folding: Matching theory and experiment

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CHEMICAL REACTION; DNA HELIX; ENTROPY; ENZYME KINETICS; PROTEIN FOLDING; PROTEIN PROCESSING; THEORY;

EID: 0031837168     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77530-7     Document Type: Article
Times cited : (50)

References (80)
  • 1
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., C. M. Jones, E. R. Henry, J. Hofrichter, and W. A. Eaton. 1992. The role of solvent viscosity in the dynamics of protein conformational changes. Science. 256:1796-1798.
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 2
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M. J., M. P. Schlunegger, and D. Eisenberg. 1995. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 3
    • 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., H. R. Halvorsen, and M. Brennan. 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    Halvorsen, H.R.2    Brennan, M.3
  • 4
    • 0029645279 scopus 로고
    • Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex
    • Bryan, P., L. Wang, J. Hoskins, S. Ruvinov, S. Strausberg, P. Alexxander, O. Almog, G. Gilliland, and T. Gallagher. 1995. Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry. 34:10310-10318.
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P.1    Wang, L.2    Hoskins, J.3    Ruvinov, S.4    Strausberg, S.5    Alexxander, P.6    Almog, O.7    Gilliland, G.8    Gallagher, T.9
  • 6
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen, B., W. A. Baase, and J. A. Schellman. 1989. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry. 28:691-699.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.1    Baase, W.A.2    Schellman, J.A.3
  • 7
    • 0018556595 scopus 로고
    • Role of proline isomerization in folding of ribonuclease a at low temperatures
    • Cook, K. H., F. X. Schmid, and R. L. Baldwin. 1979. Role of proline isomerization in folding of ribonuclease A at low temperatures. Proc. Natl. Acad. Sci. USA. 76:6157-6161.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6157-6161
    • Cook, K.H.1    Schmid, F.X.2    Baldwin, R.L.3
  • 8
    • 0016792887 scopus 로고
    • The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor
    • Creighton, T. E. 1975. The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor. J. Mol. Biol. 95: 167-199.
    • (1975) J. Mol. Biol. , vol.95 , pp. 167-199
    • Creighton, T.E.1
  • 9
    • 0029811784 scopus 로고    scopus 로고
    • Structure of the acid state of Escherichia coli ribonuclease HI
    • Dabora, J. M., J. G. Pelton, and S. Marqusee. 1996. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry. 35: 11951-11958.
    • (1996) Biochemistry , vol.35 , pp. 11951-11958
    • Dabora, J.M.1    Pelton, J.G.2    Marqusee, S.3
  • 10
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A., and H. S. Chan. 1997. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 11
    • 0029781355 scopus 로고    scopus 로고
    • The folding mechanism of larger model proteins: Role of native structure
    • Dinner, A. R., A. Sâli, and M. Karplus. 1996. The folding mechanism of larger model proteins: role of native structure. Proc. Natl. Acad. Sci. USA. 93:8356-8361.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8356-8361
    • Dinner, A.R.1    Sâli, A.2    Karplus, M.3
  • 15
  • 16
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G. A., A. K. Bhuyan, and H. Roder. 1994. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry. 33:6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 18
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 19
    • 0015715985 scopus 로고
    • Both the fast and slow refolding reactions of ribonuclease a yield native enzyme
    • Garel, J-R., and R. L. Baldwin. 1973. Both the fast and slow refolding reactions of ribonuclease A yield native enzyme. Proc. Natl. Acad. Sci. USA. 70:3347-3351.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3347-3351
    • Garel, J.-R.1    Baldwin, R.L.2
  • 20
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin, R., S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer. 1997. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:3709-3713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 21
    • 0018368942 scopus 로고
    • Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements
    • Gruenewald, B., C. U. Nicola, A. Lustig, and G. Schwarz. 1979. Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements. Biophys. Chem. 9:137-147.
    • (1979) Biophys. Chem. , vol.9 , pp. 137-147
    • Gruenewald, B.1    Nicola, C.U.2    Lustig, A.3    Schwarz, G.4
  • 22
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S. J., J. Hofrichter, A. Szabo, and W. A. Eaton. 1996. Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA. 93: 11615-11617.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 23
    • 0014691431 scopus 로고
    • Dynamics of the helix-coil transition in poly-L-ornithine
    • Hammes, G. G., and P. B. Roberts. 1969. Dynamics of the helix-coil transition in poly-L-ornithine. J. Am. Chem. Soc. 91:1812-1816.
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 1812-1816
    • Hammes, G.G.1    Roberts, P.B.2
  • 24
    • 0001756859 scopus 로고
    • Is there a single pathway for the folding of a polypeptide chain?
    • Harrison, S. C., and R. Durbin. 1985. Is there a single pathway for the folding of a polypeptide chain? Proc. Natl. Acad. Sci. USA. 82: 4028-4030.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4028-4030
    • Harrison, S.C.1    Durbin, R.2
  • 25
    • 0001842441 scopus 로고    scopus 로고
    • Adding backbone to protein folding: Proteins are polypeptides
    • Honig, B., and F. E. Cohen. 1996. Adding backbone to protein folding: proteins are polypeptides. Folding Design. 1:R17-R20.
    • (1996) Folding Design , vol.1
    • Honig, B.1    Cohen, F.E.2
  • 26
    • 0028355402 scopus 로고
    • A very fast phase in the refolding of disulfide-intact ribonuclease A: Implications for the refolding and unfolding pathways
    • Houry, W. A., D. M. Rothwarf, and H. A. Scheraga. 1994. A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways. Biochemistry. 33:2516-2530.
    • (1994) Biochemistry , vol.33 , pp. 2516-2530
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 27
    • 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., and H. A. Scheraga. 1996. Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization. Biochemistry. 35:11719-11733.
    • (1996) Biochemistry , vol.35 , pp. 11719-11733
    • Houry, W.A.1    Scheraga, H.A.2
  • 28
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson, F. M., P. E. Wright, and R. L. Baldwin. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 29
    • 0015220649 scopus 로고
    • Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins
    • Ikai, A., and C. Tanford. 1971. Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins. Nature. 230: 100-102.
    • (1971) Nature , vol.230 , pp. 100-102
    • Ikai, A.1    Tanford, C.2
  • 30
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S. E., and A. R. Fersht. 1991. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry. 30:10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 31
    • 0029904282 scopus 로고    scopus 로고
    • Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin
    • Jamin, M., and R. L. Baldwin. 1996. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. Nature Struct. Biol. 3:613-618.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 613-618
    • Jamin, M.1    Baldwin, R.L.2
  • 32
    • 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., B. E. Finn, B. E. Jones, and C. R. Matthews. 1993. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry. 32:3783-3789.
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 33
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A., and P. E. Wright. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 34
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M., and A. Sâli. 1995. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:58-73.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sâli, A.2
  • 35
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyoglobin folding intermediate
    • Kay, M. S., and R. L. Baldwin. 1996. Packing interactions in the apomyoglobin folding intermediate. Nature Struct. Biol. 3:439-445.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 439-445
    • Kay, M.S.1    Baldwin, R.L.2
  • 36
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., I. D. Peters, and H. Roder. 1996. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 37
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S., and R. L. Baldwin. 1982. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 39
    • 0026723063 scopus 로고
    • Protein folding funnels: Kinetic pathways through compact conformational space
    • Leopold, P. E., M. Montal, and J. N. Onuchic. 1992. Protein folding funnels: kinetic pathways through compact conformational space. Proc. Natl. Acad. Sci. USA. 89:8721-8725.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 40
    • 0019872826 scopus 로고
    • Effect of proline residues on protein folding
    • Levitt, M. 1981. Effect of proline residues on protein folding. J. Mol. Biol. 145:251-263.
    • (1981) J. Mol. Biol. , vol.145 , pp. 251-263
    • Levitt, M.1
  • 41
    • 0028926855 scopus 로고
    • A native tertiary interaction stabilizes the a state of cytochrome c
    • Marmorino, J. L., and G. J. Pielak. 1995. A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry. 34:3140-3143.
    • (1995) Biochemistry , vol.34 , pp. 3140-3143
    • Marmorino, J.L.1    Pielak, G.J.2
  • 42
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek, A., and A. R. Fersht. 1993. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc. Natl. Acad. Sci. USA. 90:7814-7818.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 43
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M. E., B. M. Brown, C. D. Waldburger, and R. T. Sauer. 1995. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry. 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
  • 44
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Muñoz, V., and L. Serrano. 1994. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 6:399-409.
    • (1994) Nature Struct. Biol. , vol.6 , pp. 399-409
    • Muñoz, V.1    Serrano, L.2
  • 45
    • 0029063717 scopus 로고
    • The complexity and accuracy of discrete state models of protein structure
    • Park, B. H., and M. Levitt. 1995. The complexity and accuracy of discrete state models of protein structure. J. Mol. Biol. 249:493-507.
    • (1995) J. Mol. Biol. , vol.249 , pp. 493-507
    • Park, B.H.1    Levitt, M.2
  • 46
    • 0009968319 scopus 로고
    • On the kinetics of structural transition of some pancreatic proteins
    • Pohl, F. M. 1969. On the kinetics of structural transition of some pancreatic proteins. FEBS Lett. 3:60-64.
    • (1969) FEBS Lett. , vol.3 , pp. 60-64
    • Pohl, F.M.1
  • 47
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke, T. M., and S. Marqusee. 1997. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol. 4:298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 48
    • 0029954416 scopus 로고    scopus 로고
    • Deterministic pressure dissociation and unfolding of triose phosphate isomerase: Persistent heterogeneity of a protein dimer
    • Rietveld, A. W. M., and S. T. Ferreira. 1996. Deterministic pressure dissociation and unfolding of triose phosphate isomerase: persistent heterogeneity of a protein dimer. Biochemistry. 35:7743-7751.
    • (1996) Biochemistry , vol.35 , pp. 7743-7751
    • Rietveld, A.W.M.1    Ferreira, S.T.2
  • 49
    • 0029961470 scopus 로고    scopus 로고
    • Equilibrium stability and submillisecond refolding of a designed single-chain Arc repressor
    • Robinson, C. R., and R. T. Sauer. 1996. Equilibrium stability and submillisecond refolding of a designed single-chain Arc repressor. Biochemistry. 35:13878-13884.
    • (1996) Biochemistry , vol.35 , pp. 13878-13884
    • Robinson, C.R.1    Sauer, R.T.2
  • 50
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L.
    • Scalley, M. L., Q. Yi, H. Gu, A. McCormack, J. R. Yates III, and D. Baker. 1997. Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L. Biochemistry. 36:3373-3382.
    • (1997) Biochemistry , vol.36 , pp. 3373-3382
    • Scalley, M.L.1    Yi, Q.2    Gu, H.3    McCormack, A.4    Yates J.R. III5    Baker, D.6
  • 51
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler, T., and F. X. Schmid. 1996. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry. 35: 16833-16842.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 52
    • 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
  • 53
    • 0018143763 scopus 로고
    • Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization
    • Schmid, F. X., and R. L. Baldwin. 1978. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc. Natl. Acad. Sci. USA. 75:4764-4768.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4764-4768
    • Schmid, F.X.1    Baldwin, R.L.2
  • 54
    • 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., and H. Blaschek. 1981. A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. Eur. J. Biochem. 114:111-117.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 111-117
    • Schmid, F.X.1    Blaschek, H.2
  • 55
    • 0029765444 scopus 로고    scopus 로고
    • Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
    • Schulman, B. A., and P. S. Kim. 1996. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. Nature Struct. Biol. 3:682-687.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 56
    • 78651171134 scopus 로고
    • On the kinetics of the helix-coil transition of polypeptides in solution
    • Schwarz, G. 1965. On the kinetics of the helix-coil transition of polypeptides in solution. J. Mol. Biol. 11:64-77.
    • (1965) J. Mol. Biol. , vol.11 , pp. 64-77
    • Schwarz, G.1
  • 57
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., V. Abkevich, and O. Ptitsyn. 1996. Conserved residues and the mechanism of protein folding. Nature. 379:96-98.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 58
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow, M., and M. Oliveberg. 1997. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl. Acad. Sci. USA. 94:6084-6086.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 59
    • 0028426938 scopus 로고
    • Kinetic partitioning during protein folding yields multiple native states
    • Sinclair, J. F., M. M. Ziegler, and T. O. Baldwin. 1994. Kinetic partitioning during protein folding yields multiple native states. Nature Struct. Biol. 1:320-326.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 320-326
    • Sinclair, J.F.1    Ziegler, M.M.2    Baldwin, T.O.3
  • 61
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T. R., L. Mayne, and S. W. Englander. 1996b. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins Struct. Funct. Genet. 24:413-426.
    • (1996) Proteins Struct. Funct. Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 64
    • 0029911537 scopus 로고    scopus 로고
    • In vitro renaturation of bovine β-lactoglobulin a leads to a biologically active but incompletely refolded state
    • Subramaniam, V., D. G. Steel, and A. Gafni. 1996. In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state. Protein Sci. 5:2089-2094.
    • (1996) Protein Sci. , vol.5 , pp. 2089-2094
    • Subramaniam, V.1    Steel, D.G.2    Gafni, A.3
  • 66
    • 0014718113 scopus 로고
    • Theoretical models for the mechanism of denaturation
    • Tanford, C. 1970. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 67
    • 0030743517 scopus 로고    scopus 로고
    • Temperature control for kinetic refolding of heat-denatured ovalbumin
    • Tani, F., N. Shirai, T. Onishi, F. Venelle, K. Yasumoto, and E. Doi. 1997. Temperature control for kinetic refolding of heat-denatured ovalbumin. Protein Sci. 6:1491-1502.
    • (1997) Protein Sci. , vol.6 , pp. 1491-1502
    • Tani, F.1    Shirai, N.2    Onishi, T.3    Venelle, F.4    Yasumoto, K.5    Doi, E.6
  • 69
    • 0015506093 scopus 로고
    • Kinetic evidence for intermediate states in the unfolding of chymotrypsinogen A
    • Tsong, T. Y., and R. L. Baldwin. 1972. Kinetic evidence for intermediate states in the unfolding of chymotrypsinogen A. J. Mol. Biol. 69: 145-148.
    • (1972) J. Mol. Biol. , vol.69 , pp. 145-148
    • Tsong, T.Y.1    Baldwin, R.L.2
  • 70
    • 0015155644 scopus 로고
    • The sequential unfolding of ribonuclease A: Detection of a fast initial phase in the kinetics of unfolding
    • Tsong, T. Y., R. L. Baldwin, and E. L. Elson. 1971. The sequential unfolding of ribonuclease A: detection of a fast initial phase in the kinetics of unfolding. Proc. Natl. Acad. Sci. USA. 68:2712-2715.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2712-2715
    • Tsong, T.Y.1    Baldwin, R.L.2    Elson, E.L.3
  • 71
    • 0015505381 scopus 로고
    • A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A
    • Tsong, T. Y., R. L. Baldwin, and P. McPhie. 1972. A sequential model of nucleation-dependent protein folding: kinetic studies of ribonuclease A. J. Mol. Biol. 63:453-475.
    • (1972) J. Mol. Biol. , vol.63 , pp. 453-475
    • Tsong, T.Y.1    Baldwin, R.L.2    McPhie, P.3
  • 72
    • 0030475698 scopus 로고    scopus 로고
    • Kinetically controlled folding of the serpin plasminogen activator inhibitor 1
    • Wang, Z., J. Mottonen, and E. J. Goldsmith. 1996. Kinetically controlled folding of the serpin plasminogen activator inhibitor 1. Biochemistry. 35:16443-16448.
    • (1996) Biochemistry , vol.35 , pp. 16443-16448
    • Wang, Z.1    Mottonen, J.2    Goldsmith, E.J.3
  • 73
    • 0023051838 scopus 로고
    • Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and of hydrostatic pressure
    • Weber, G. 1986. Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and of hydrostatic pressure. Biochemistry. 25:3626-3631.
    • (1986) Biochemistry , vol.25 , pp. 3626-3631
    • Weber, G.1
  • 74
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper
    • Wendt, H., L. Leder, H. Härmä, I. Jelesarov, A. Baici, and H. R. Bosshard. 1997. Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry. 36:204-213.
    • (1997) Biochemistry , vol.36 , pp. 204-213
    • Wendt, H.1    Leder, L.2    Härmä, H.3    Jelesarov, I.4    Baici, A.5    Bosshard, H.R.6
  • 75
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G., and T. Kiefhaber. 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
  • 78
    • 0009672359 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, R. H., and J. K. Bragg. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:476-485.
    • (1959) J. Chem. Phys. , vol.31 , pp. 476-485
    • Zimm, R.H.1    Bragg, J.K.2
  • 79
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • Zwanzig, R. 1995. Simple model of protein folding kinetics. Proc. Natl. Acad Sci. USA. 92:9801-9804.
    • (1995) Proc. Natl. Acad Sci. USA , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 80
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models of protein folding kinetics
    • Zwanzig, R. 1997. Two-state models of protein folding kinetics. Proc. Natl. Acad. Sci. USA. 94:148-150.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 148-150
    • Zwanzig, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.