메뉴 건너뛰기




Volumn 3, Issue 4, 1998, Pages

How do small single-domain proteins fold?

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; CHYMOTRYPSIN INHIBITOR; CYTOCHROME C; FODRIN; TENASCIN; UBIQUITIN;

EID: 0031815749     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00033-9     Document Type: Article
Times cited : (867)

References (88)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. (1968). Are there pathways for protein folding? J. Chim. Phys. 85, 44-45.
    • (1968) J. Chim. Phys. , vol.85 , pp. 44-45
    • Levinthal, C.1
  • 2
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S. & Baldwin, R.L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 3
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. & Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 4
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 1. Evidence for a two-state transition
    • Jackson, S.E. & Fersht, A.R. (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
  • 5
    • 0028935887 scopus 로고
    • Structure and stability of monomeric λ represser: NMR evidence for two-state folding
    • Huang, G.S. & Oas, T.G. (1995). Structure and stability of monomeric λ represser: NMR evidence for two-state folding. Biochemistry 34, 3884-3892.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 7
  • 8
    • 0029965111 scopus 로고    scopus 로고
    • Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family
    • Kragelund, B.B., et al., & Poulsen, P.M. (1996). Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family. J. Mol. Biol. 256, 187-200.
    • (1996) J. Mol. Biol. , vol.256 , pp. 187-200
    • Kragelund, B.B.1    Poulsen, P.M.2
  • 9
    • 0031047914 scopus 로고    scopus 로고
    • Submillisecond protein folding kinetics studied by ultrarapid mixing
    • Chan, C.K., et al., & Hofrichter, J. (1997). Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc. Natl Acad. Sci. USA 94, 1779-1784.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1779-1784
    • Chan, C.K.1    Hofrichter, J.2
  • 11
    • 0038933138 scopus 로고    scopus 로고
    • Folding of the disulfide-bonded β-sheet protein tendamistat: Rapid two-state folding without hydrophobic collapse
    • Schonbrunner, N., Koller, K.-P. & Kiefhaber, T. (1997). Folding of the disulfide-bonded β-sheet protein tendamistat: rapid two-state folding without hydrophobic collapse. J. Mol. Biol. 268, 526-538.
    • (1997) J. Mol. Biol. , vol.268 , pp. 526-538
    • Schonbrunner, N.1    Koller, K.-P.2    Kiefhaber, T.3
  • 13
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D., et al., & Schmid, F.X. (1998). Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct Biol. 5, 229-235.
    • (1998) Nat. Struct Biol. , vol.5 , pp. 229-235
    • Perl, D.1    Schmid, F.X.2
  • 14
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model β-sheet protein, Escherichia coli CspA
    • Reid, K.L., Rodriguez, H.M., Hillier, B.J. & Gregoret, L.M. (1998). Stability and folding properties of a model β-sheet protein, Escherichia coli CspA. Protein Sci. 7, 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
  • 15
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic-analysis of the SH3 domain of spectrin shows a 2-state folding transition
    • Viguera, A., Martinez, J., Filimonov, V., Mateo, P. & Serrano, L. (1994). Thermodynamic and kinetic-analysis of the SH3 domain of spectrin shows a 2-state folding transition. Biochemistry 33, 2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.1    Martinez, J.2    Filimonov, V.3    Mateo, P.4    Serrano, L.5
  • 16
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition-states may result in the same native structure
    • Viguera, A.R., Serrano, L. & Wilmanns, M. (1996). Different folding transition-states may result in the same native structure. Nat. Struct. Biol. 3, 874-880.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 17
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the src SH3 domain
    • Grantcharova, V.P. & Baker, D. (1997). Folding dynamics of the src SH3 domain. Biochemistry 36, 15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 18
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy
    • Guijarro, J.I., Morton, C.J., Plaxco, K.W., Campbell, I.D. & Dobson, C.M. (1998). Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J. Mol. Biol. 276, 657-667.
    • (1998) J. Mol. Biol. , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 19
    • 0032562182 scopus 로고    scopus 로고
    • The folding kinetics and thermodynamics of the Fyn-SH3 domain
    • Plaxco, K.W., et al., & Dobson, C.M. (1998). The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 37, 2529-2537.
    • (1998) Biochemistry , vol.37 , pp. 2529-2537
    • Plaxco, K.W.1    Dobson, C.M.2
  • 20
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodyanmics of two homologous fibronectin type III modules
    • Plaxco, K.W., Spitzfaden, C., Campbell, I.D. & Dobson, C.M. (1997). A comparison of the folding kinetics and thermodyanmics of two homologous fibronectin type III modules. J. Mol. Biol. 270, 763-770.
    • (1997) J. Mol. Biol. , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 21
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • Clarke, J., Hamill, S.J. & Johnson, C.M. (1997). Folding and stability of a fibronectin type III domain of human tenascin. J. Mol. Biol. 270, 771-778.
    • (1997) J. Mol. Biol. , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 22
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas, V., et al., & Serrano, L. (1995). Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 34, 15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Serrano, L.2
  • 23
    • 0029961470 scopus 로고    scopus 로고
    • Equilibrium stability and submillisecond refolding of a designed single-chain Arc repressor
    • Robinson, C.R. & Sauer, R.T. (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
  • 24
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh, S., Peters, I.D., Butt, T.R. & Roder, H. (1993). Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry 32, 7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 25
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I.D. & Roder, H. (1996). Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. 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
  • 26
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptococcal protein L
    • Scalley, M.L., et al., & Baker, D. (1997). Kinetics of folding of the IgG binding domain of peptostreptococcal protein L. Biochemistry 36, 3373-3382.
    • (1997) Biochemistry , vol.36 , pp. 3373-3382
    • Scalley, M.L.1    Baker, D.2
  • 27
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow, M. & Oliveberg, M. (1997). High-energy channeling in protein folding. Biochemistry 36, 7633-7636.
    • (1997) Biochemistry , vol.36 , pp. 7633-7636
    • Silow, M.1    Oliveberg, M.2
  • 28
    • 0032512440 scopus 로고    scopus 로고
    • Slow co-operative folding of a small globular protein HPr
    • van Nuland, N.A.J., et al., & Dobson, C.M. (1998). Slow co-operative folding of a small globular protein HPr. Biochemistry 37, 622-637.
    • (1998) Biochemistry , vol.37 , pp. 622-637
    • Van Nuland, N.A.J.1    Dobson, C.M.2
  • 29
    • 0032491565 scopus 로고    scopus 로고
    • Slow folding of muscle acylphosphatase in the absence of intermediates
    • in press
    • van Nuland, N.A.J., et al., & Dobson, C.M. (1998). Slow folding of muscle acylphosphatase in the absence of intermediates. J. Mol. Biol., in press.
    • (1998) J. Mol. Biol.
    • Van Nuland, N.A.J.1    Dobson, C.M.2
  • 30
    • 0032514727 scopus 로고    scopus 로고
    • Folding kinetics of villin 14T, a protein domain with a central β-sheet and two hydrophobic cores
    • in press
    • Choe, S.E., Matsudaira, P.T., Osterhout, J., Wagner, G. & Shakhnovich, E.I. (1998) Folding kinetics of villin 14T, a protein domain with a central β-sheet and two hydrophobic cores. Biochemistry, in press.
    • (1998) Biochemistry
    • Choe, S.E.1    Matsudaira, P.T.2    Osterhout, J.3    Wagner, G.4    Shakhnovich, E.I.5
  • 31
    • 0032474435 scopus 로고    scopus 로고
    • The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin
    • Hamill, S.J., Meekhof, A.E. & Clarke, J. (1998). The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin. Biochemistry 37, 8071-8079.
    • (1998) Biochemistry , vol.37 , pp. 8071-8079
    • Hamill, S.J.1    Meekhof, A.E.2    Clarke, J.3
  • 32
    • 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., & Fersht, A.R. (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
  • 34
    • 0032584281 scopus 로고    scopus 로고
    • Movement of the intermediate and rate-determining transition state of barnase on the energy landscape with changing temperature
    • Dalby, P.A., Oliveberg, M. & Fersht, A.R. (1998). Movement of the intermediate and rate-determining transition state of barnase on the energy landscape with changing temperature. Biochemistry 37, 4674-4679.
    • (1998) Biochemistry , vol.37 , pp. 4674-4679
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 35
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-279.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 36
    • 0032570757 scopus 로고    scopus 로고
    • Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate
    • Dalby, P.A., Clarke, J., Johnson, C.M. & Fersht, A.R. (1998). Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate. J. Mol. Biol. 276, 647-656.
    • (1998) J. Mol. Biol. , vol.276 , pp. 647-656
    • Dalby, P.A.1    Clarke, J.2    Johnson, C.M.3    Fersht, A.R.4
  • 37
    • 0032570532 scopus 로고    scopus 로고
    • Folding intermediates of wild-type and mutants of barnase. I. Use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium
    • Dalby, P.A., Oliveberg, M. & Fersht, A.R. (1998). Folding intermediates of wild-type and mutants of barnase. I. Use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium. J. Mol. Biol. 276, 625-646.
    • (1998) J. Mol. Biol. , vol.276 , pp. 625-646
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 38
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T. & Baker, D. (1998). Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 39
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C.M., Sali, A. & Karplus, M. (1998). Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. Engl. 37, 868-893.
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 40
    • 0002682169 scopus 로고    scopus 로고
    • Local versus nonlocal interactions in protein folding and stability - An experimentalist's point of view
    • Munoz, V. & Serrano, L. (1996). Local versus nonlocal interactions in protein folding and stability - an experimentalist's point of view. Fold. Des. 1; R71-R77.
    • (1996) Fold. Des. , vol.1
    • Munoz, V.1    Serrano, L.2
  • 41
    • 0030272670 scopus 로고    scopus 로고
    • Time-resolved biophysical methods in the study of protein-folding
    • Plaxco, K.W. & Dobson, C.M. (1996). Time-resolved biophysical methods in the study of protein-folding. Curr. Opin. Struct. Biol. 6, 630-636.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 630-636
    • Plaxco, K.W.1    Dobson, C.M.2
  • 42
    • 0027770910 scopus 로고
    • Detection of transient protein-folding populations by mass-spectrometry
    • Miranker, A., Robinson, C.V., Radford, S.E., Aplin, R.T. & Dobson, C.M. (1993). Detection of transient protein-folding populations by mass-spectrometry. Science 262, 896-900.
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 43
    • 0029151862 scopus 로고
    • Cooperative elements in protein-folding monitored by electrospray-ionization mass-spectrometry
    • Hooke, S.D., et al., & Dobson, C.M. (1995). Cooperative elements in protein-folding monitored by electrospray-ionization mass-spectrometry. J. Am. Chem. Soc. 117, 7548-7549.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7548-7549
    • Hooke, S.D.1    Dobson, C.M.2
  • 44
    • 0030027339 scopus 로고    scopus 로고
    • Investigation of protein-folding by mass-spectrometry
    • Miranker, A., Robinson, C.V., Radford, S.E. & Dobson, C.M. (1996). Investigation of protein-folding by mass-spectrometry. FASEB J. 10, 93-101.
    • (1996) FASEB J. , vol.10 , pp. 93-101
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Dobson, C.M.4
  • 45
    • 0032491469 scopus 로고    scopus 로고
    • Structural characterisation of the transition state for folding of muscle acylphophatase
    • in press
    • Chiti, F., et al., & Dobson, C.M. (1998). Structural characterisation of the transition state for folding of muscle acylphophatase. J. Mol. Biol., in press.
    • (1998) J. Mol. Biol.
    • Chiti, F.1    Dobson, C.M.2
  • 46
    • 0026511656 scopus 로고
    • The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., Matouschek, A. & Serrano, L. (1992). The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 48
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., Yao, J., Dyson, H.J. & Wright, P.E. (1998). Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5, 148-155.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 49
    • 0032555115 scopus 로고    scopus 로고
    • Synergy between simulation and experiment in describing the energy landscape of protein folding
    • in press
    • Ladurner, A.G., Itzhaki, L.S., Daggett, V. & Fersht, A.R. (1998). Synergy between simulation and experiment in describing the energy landscape of protein folding. Proc. Natl Acad. Sci. USA, in press.
    • (1998) Proc. Natl Acad. Sci. USA
    • Ladurner, A.G.1    Itzhaki, L.S.2    Daggett, V.3    Fersht, A.R.4
  • 50
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • Jackson, S.E., elMasry, N. & Fersht, A.R. (1993). Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. Biochemistry 32, 11270-11278.
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    ElMasry, N.2    Fersht, A.R.3
  • 51
    • 0030627747 scopus 로고    scopus 로고
    • Speeding up protein folding: Mutations that increase the rate at which ROP folds and unfolds by over four orders of magnitude
    • Munson, M., Anderson, K.S. & Regan, L. (1997). Speeding up protein folding: mutations that increase the rate at which ROP folds and unfolds by over four orders of magnitude. Fold. Des. 2, 77-87.
    • (1997) Fold. Des. , vol.2 , pp. 77-87
    • Munson, M.1    Anderson, K.S.2    Regan, L.3
  • 52
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R.L (1996). On-pathway versus off-pathway folding intermediates. Fold. Des. 1, R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 53
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-collapse mechanism for the folding of chymotrypsin inhibitor 2 (Cl2) and its consequences
    • Fersht, A.R. (1995). Optimization of rates of protein folding: the nucleation-collapse mechanism for the folding of chymotrypsin inhibitor 2 (Cl2) and its consequences. Proc. Natl Acad. Sci. USA 92, 10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 54
    • 0027385015 scopus 로고
    • The refolding of cis-peptidylprolyl and trans-peptidylprolyl isomers of barstar
    • Schreiber, G. & Fersht, A.R. (1993). The refolding of cis-peptidylprolyl and trans-peptidylprolyl isomers of barstar. Biochemistry 32, 11195-11203.
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 55
    • 0030871209 scopus 로고    scopus 로고
    • Acquisition of native β-strand topolgy during the rapid collapse phase of protein folding
    • Parker, M., Dempsey, C.E., Lorch, M. & Clarke, A.R. (1997). Acquisition of native β-strand topolgy during the rapid collapse phase of protein folding. Biochemistry 36, 13396-13405.
    • (1997) Biochemistry , vol.36 , pp. 13396-13405
    • Parker, M.1    Dempsey, C.E.2    Lorch, M.3    Clarke, A.R.4
  • 56
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., Kellis, J.T., Jr, Serrano, L., Bycroft, M. & Fersht, A.R. (1990). Transient folding intermediates characterized by protein engineering. Nature 346, 440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 57
    • 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
  • 58
    • 0028791393 scopus 로고
    • An integrated kineticanalysis of intermediates and transition-states in protein-folding reactions
    • Parker, M.J., Spencer, J. & Clarke, A.R. (1995). An integrated kineticanalysis of intermediates and transition-states in protein-folding reactions. J. Mol. Biol. 253, 771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 59
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from Escherichia coli, CheY - Kinetic-analysis of the inverse hydrophobic effect
    • Munoz, V., Lopez, E.M., Jager, M. & Serrano, L. (1994). Kinetic characterization of the chemotactic protein from Escherichia coli, CheY - kinetic-analysis of the inverse hydrophobic effect. Biochemistry 33, 5858-5866.
    • (1994) Biochemistry , vol.33 , pp. 5858-5866
    • Munoz, V.1    Lopez, E.M.2    Jager, M.3    Serrano, L.4
  • 60
    • 0032548994 scopus 로고    scopus 로고
    • Thermodynamic stability and folding of GroEL minichaperones
    • Golbik, R., Zahn, R., Harding, S.E. & Fersht, A.R. (1998). Thermodynamic stability and folding of GroEL minichaperones. J. Mol. Biol. 276, 505-515.
    • (1998) J. Mol. Biol. , vol.276 , pp. 505-515
    • Golbik, R.1    Zahn, R.2    Harding, S.E.3    Fersht, A.R.4
  • 61
    • 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. & Marqusee, S. (1997). The kinetic folding intermediate of ribonuclease h resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat. Struct. Biol. 4, 298-304.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 62
    • 0029598779 scopus 로고
    • Folding pathway of Escherichia coli ribonuclease HI: A circular dichroism, fluorescence and NMR study
    • Yamasaki, K., Ogagahara, K., Yutani, K., Oobatake, M. & Kanaya, S. (1995). Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence and NMR study. Biochemistry 34, 16552-16562.
    • (1995) Biochemistry , vol.34 , pp. 16552-16562
    • Yamasaki, K.1    Ogagahara, K.2    Yutani, K.3    Oobatake, M.4    Kanaya, S.5
  • 63
    • 0030347884 scopus 로고    scopus 로고
    • The development of tertiary interactions during the folding of a large protein
    • Parker, M.J., Sessions, R.B., Badcoe, I.G. & Clarke, A.R. (1996). The development of tertiary interactions during the folding of a large protein. Fold. Des. 1, 145-156.
    • (1996) Fold. Des. , vol.1 , pp. 145-156
    • Parker, M.J.1    Sessions, R.B.2    Badcoe, I.G.3    Clarke, A.R.4
  • 64
    • 0030023486 scopus 로고    scopus 로고
    • The roles of partly folded intermediates in protein folding
    • Creighton, T.E., Darby, N.J. & Kemmink, J. (1996). The roles of partly folded intermediates in protein folding. FASEB. J. 10, 110-118.
    • (1996) FASEB. J. , vol.10 , pp. 110-118
    • Creighton, T.E.1    Darby, N.J.2    Kemmink, J.3
  • 65
    • 0031205431 scopus 로고    scopus 로고
    • Protein folding pathways and intermediates
    • Clarke, A.R. & Waltho, J.P. (1997). Protein folding pathways and intermediates. Curr. Opin. Biotechnol. 8, 400-410.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 400-410
    • Clarke, A.R.1    Waltho, J.P.2
  • 66
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colon, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 67
    • 0029157429 scopus 로고
    • Compact intermediate states in protein-folding
    • Fink, A.L. (1995). Compact intermediate states in protein-folding. Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 68
    • 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
  • 69
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome-c folding - Involvement of the heme and its ligands
    • Elove, G.A., Bhuyan, A.K. & Roder, H. (1994). Kinetic mechanism of cytochrome-c folding - involvement of the heme and its ligands. Biochemistry 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elove, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 70
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme ligation
    • Hammack, B., Godbole, S. & Bowler, B.E. (1998). Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation. J. Mol. Biol. 275, 719-724.
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 71
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse - The rate-limiting step in 2-state cytochrome-c folding
    • Sosnick, T.R., Mayne, L. & Englander, S.W. (1996). Molecular collapse - the rate-limiting step in 2-state cytochrome-c folding. Proteins 24, 413-426.
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 73
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
    • Matagne, A., Radford, S.E. & Dobson, C.M. (1997). Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process. J. Mol. Biol. 267, 1068-1074.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 74
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S.E., Dobson, C.M. & Evans, P.A. (1992). The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 75
    • 0031575421 scopus 로고    scopus 로고
    • Acceleration of the folding of hen lysozyme by trifluoroethanol
    • Lu, H., Buck, M., Radford, S.E. & Dobson, C.M. (1997). Acceleration of the folding of hen lysozyme by trifluoroethanol. J. Mol. Biol. 265, 112-117.
    • (1997) J. Mol. Biol. , vol.265 , pp. 112-117
    • Lu, H.1    Buck, M.2    Radford, S.E.3    Dobson, C.M.4
  • 76
    • 13244294100 scopus 로고
    • Catalysis and assistance of protein folding
    • Schmid, F.X. (1991). Catalysis and assistance of protein folding. Curr. Opin. Struct. Biol. 1, 36-41.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 36-41
    • Schmid, F.X.1
  • 77
    • 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., Rothwarf, D.M. & Scheraga, H.A. (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
  • 78
    • 0028325298 scopus 로고
    • P22 arc repressor - Folding kinetics of a single-domain, dimeric protein
    • Milla, M. & Sauer, R. (1994). P22 arc repressor - folding kinetics of a single-domain, dimeric protein. Biochemistry 33, 1125-1133.
    • (1994) Biochemistry , vol.33 , pp. 1125-1133
    • Milla, M.1    Sauer, R.2
  • 79
    • 0028952291 scopus 로고
    • Crystal-structure, folding, and operator binding of the hyperstable arc repressor mutant PLI8
    • Schildbach, J.F., Milla, M.E., Jeffrey, P.D., Raumann, B.E. & Sauer, R.T. (1995). Crystal-structure, folding, and operator binding of the hyperstable arc repressor mutant PLI8. Biochemistry 34, 1405-1412.
    • (1995) Biochemistry , vol.34 , pp. 1405-1412
    • Schildbach, J.F.1    Milla, M.E.2    Jeffrey, P.D.3    Raumann, B.E.4    Sauer, R.T.5
  • 80
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein-folding - Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger, C.D., Jonsson, T. & Sauer, R.T. (1996). Barriers to protein-folding - formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl Acad. Sci. USA 93, 2629-2634.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 81
    • 4243067681 scopus 로고    scopus 로고
    • Protein stabilization by removal of unsatisfied polar groups - Computational approaches and experimental tests
    • Hendsch, Z.S., Jonsson, T., Sauer, R.T. & Tidor, B. (1996). Protein stabilization by removal of unsatisfied polar groups - computational approaches and experimental tests. Biochemistry 35, 7621-7625.
    • (1996) Biochemistry , vol.35 , pp. 7621-7625
    • Hendsch, Z.S.1    Jonsson, T.2    Sauer, R.T.3    Tidor, B.4
  • 82
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine-zipper peptide by stopped-flow circular-dichroism spectroscopy
    • Zitzewitz, J.A., Bilsel, O., Luo, J.B., Jones, B.E. & Matthews, C.R. (1995). Probing the folding mechanism of a leucine-zipper peptide by stopped-flow circular-dichroism spectroscopy. Biochemistry 34, 12812-12819.
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.B.3    Jones, B.E.4    Matthews, C.R.5
  • 83
    • 0026579572 scopus 로고
    • The folding of an enzyme. 3. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
    • Serrano, L., Matouschek, A. & Fersht, A.R. (1992). The folding of an enzyme. 3. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224, 805-818.
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 84
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-collapse mechanism for protein folding
    • Itzhaki, L.S., Otzen, D.E. & Fersht, A.R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-collapse mechanism for protein folding. J. Mol. Biol. 254, 260-288
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 85
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera, A.R., Blanco, F.J. & Serrano, L. (1995). The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247, 670-681.
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 86
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, Cl-2
    • Lopez-Hernandez, E. & Serrano, L. (1996). Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, Cl-2. Fold. Des. 1, 43-55.
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 87
    • 0029653905 scopus 로고
    • Mapping the structures of transition-states and intermediates in folding - Delineation of pathways at high-resolution
    • Fersht, A.R. (1995). Mapping the structures of transition-states and intermediates in folding - delineation of pathways at high-resolution. Philos. Trans. R. Soc. Lond. B Biol. Sci. 348, 11-15.
    • (1995) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.348 , pp. 11-15
    • Fersht, A.R.1
  • 88
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • Viguera, A.R., Villegas, V., Aviles, F.X. & Serrano, L. (1997). Favourable native-like helical local interactions can accelerate protein folding. Fold. Des. 2, 23-33.
    • (1997) Fold. Des. , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Aviles, F.X.3    Serrano, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.