메뉴 건너뛰기




Volumn 4, Issue 12, 1997, Pages 1016-1024

Multiple intermediates and transition states during protein unfolding

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

EID: 0030787174     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1297-1016     Document Type: Article
Times cited : (103)

References (46)
  • 1
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho, C. J. & Thirumalai, D. Kinetics and thermodynamics of folding in model proteins. Proc. Natl. Acad. Sci. USA 90, 6369-6372 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 2
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H. S. & Dill, K. A. Transition states and folding dynamics of proteins and heteropolymers. J. Chem Phys. 100, 9238-9257 (1994).
    • (1994) J. Chem Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 5
    • 0028776642 scopus 로고
    • Matching speed and stability
    • Baldwin, R. L. Matching speed and stability. Nature 369, 183-184 (1994).
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 6
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R. L. The nature of protein folding pathways: The classical versus the new view. J. Biomolec. NMR 5, 103-109 (1995).
    • (1995) J. Biomolec. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 7
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. & Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 8
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding, I. Effect of protein-solvent interactions on the transition state
    • Segawa, S. & Sugihara, M. Characterization of the transition state of lysozyme unfolding, I. Effect of protein-solvent interactions on the transition state. Biopolymers 23, 2473-2488 (1984).
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.1    Sugihara, M.2
  • 9
    • 0024596024 scopus 로고
    • 2+ binding on the folding kinetics of alpha-lactalbumin
    • 2+ binding on the folding kinetics of alpha-lactalbumin. J. Mol. Biol. 206, 547-561 (1989).
    • (1989) J. Mol. Biol. , vol.206 , pp. 547-561
    • Kuwajima, K.1    Mitani, M.2    Sugai, S.3
  • 10
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen, B. L., Baase, W. A. & Schellman, J. A. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28, 691-699 (1989).
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 11
    • 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 31, 1464-1476 (1992).
    • (1992) Biochemistry , vol.31 , pp. 1464-1476
    • Chen, B.L.1    Baase, W.A.2    Nicholson, H.3    Schellman, J.A.4
  • 12
    • 0028271856 scopus 로고
    • Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase
    • Chen, X. W. & Matthews, C. R. Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry 33, 6356-6362 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6356-6362
    • Chen, X.W.1    Matthews, C.R.2
  • 13
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg, M., Tan, Y. -J. & Fersht, A. R. Negative activation enthalpies in the kinetics of protein folding. Proc. Natl. Acad. Sci. U.S.A. 92, 8926-8929 (1995).
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 14
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan, Y.-J., Oliveberg, M. & Fersht, A. R. Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264, 377-389 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.-J.1    Oliveberg, M.2    Fersht, A.R.3
  • 15
    • 0030882667 scopus 로고    scopus 로고
    • Thermodynamics of the complex protein unfolding reaction of barstar
    • Agashe, V. R., Schmid, F. X. & Udgaonkar, J. B. Thermodynamics of the complex protein unfolding reaction of barstar. Biochemistry 36, 12288-12295 (1997).
    • (1997) Biochemistry , vol.36 , pp. 12288-12295
    • Agashe, V.R.1    Schmid, F.X.2    Udgaonkar, J.B.3
  • 16
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek, A., Kellis, J. T., Jr., Serrano, L. & Fersht, A. R. Mapping the transition state and pathway of protein folding by protein engineering. Nature 342, 122-126 (1989).
    • (1989) Nature , vol.342 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 17
  • 18
    • 0029001090 scopus 로고
    • Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • Kiefhaber, T., Labhardt, A. M. & Baldwin, R. L. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375, 513-515 (1995).
    • (1995) Nature , vol.375 , pp. 513-515
    • Kiefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 19
    • 0029079665 scopus 로고
    • 19F-tryptophan-labeled Escherichia coli dihydrofolate reductase
    • 19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. Proc. Natl. Acad. Sci. USA 92, 9318-9322 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9318-9322
    • Hoeltzli, S.D.1    Frieden, C.2
  • 20
    • 0000067372 scopus 로고    scopus 로고
    • How do proteins fold?
    • Nath, U. & Udgaonkar, J. B. How do proteins fold? Curr. Sci. 72, 180-191 (1997).
    • (1997) Curr. Sci. , vol.72 , pp. 180-191
    • Nath, U.1    Udgaonkar, J.B.2
  • 21
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colón, W. Kinetic role of early intermediates in protein folding. Curr Opin. Struct. Biol. 7, 15-28 (1997).
    • (1997) Curr Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 22
    • 0027385015 scopus 로고
    • The refolding of cis- and trans-peptidylprolyl isomers of barstar
    • Schreiber, G. & Fersht, A. R. The refolding of cis- and trans-peptidylprolyl isomers of barstar. Biochemistry 32, 11195-11203 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 23
    • 0028072360 scopus 로고
    • Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone
    • Shastry, M. C. R., Agashe, V. R. & Udgaonkar, J. B. Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone. Protein Science 3, 1409-1417 (1994).
    • (1994) Protein Science , vol.3 , pp. 1409-1417
    • Shastry, M.C.R.1    Agashe, V.R.2    Udgaonkar, J.B.3
  • 24
    • 0028901085 scopus 로고
    • The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates
    • Shastry, M. C. R. & Udgaonkar, J. B. The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates. J. Mol. Biol. 247, 1013-1027 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013-1027
    • Shastry, M.C.R.1    Udgaonkar, J.B.2
  • 25
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe, V. R., Shastry, M. C. R. & Udgaonkar, J. B. Initial hydrophobic collapse in the folding of barstar. Nature 377, 754-757 (1995).
    • (1995) Nature , vol.377 , pp. 754-757
    • Agashe, V.R.1    Shastry, M.C.R.2    Udgaonkar, J.B.3
  • 27
    • 0031019924 scopus 로고    scopus 로고
    • The folding pathway of a protein at high resolution from microseconds to seconds
    • Nölting, B. et al. The folding pathway of a protein at high resolution from microseconds to seconds. Proc. Natl. Acad. Sci. USA 94, 826-830 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 826-830
    • Nölting, B.1
  • 28
    • 0030740123 scopus 로고    scopus 로고
    • Folding of tryptophan mutants of barstar: Evidence for an initial hydrophobic collapse on the folding pathway
    • Math, U. & Udgaonkar, J. B. Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway. Biochemistry 36, 8602-8610 (1997).
    • (1997) Biochemistry , vol.36 , pp. 8602-8610
    • Math, U.1    Udgaonkar, J.B.2
  • 29
    • 0029908737 scopus 로고    scopus 로고
    • Initial Loss of secondary structure in the unfolding of barstar
    • Nath, U., Agashe, V. R. & Udgaonkar, J. B. Initial Loss of secondary structure in the unfolding of barstar Nature Struct. Biol. 3, 920-923 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 920-923
    • Nath, U.1    Agashe, V.R.2    Udgaonkar, J.B.3
  • 31
    • 0029868589 scopus 로고    scopus 로고
    • Nonlinear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates
    • Jonsson, T., Waldburger, C. D. & Sauer, R. T. Nonlinear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates. Biochemistry 35, 4795-4802 (1996).
    • (1996) Biochemistry , vol.35 , pp. 4795-4802
    • Jonsson, T.1    Waldburger, C.D.2    Sauer, R.T.3
  • 32
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability?
    • Baldwin, R. L. How Hofmeister ion interactions affect protein stability? Biophysical J. 71, 2056-2063 (1996).
    • (1996) Biophysical J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 33
    • 0028947236 scopus 로고
    • Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
    • Agashe, V. R. & Udgaonkar, J. B. Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry 34, 3286-3299 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3286-3299
    • Agashe, V.R.1    Udgaonkar, J.B.2
  • 34
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin, R. L. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA 83, 8069-8072 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 35
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L. S., Qtzen, D. E. & Fersht, A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Qtzen, D.E.2    Fersht, A.R.3
  • 36
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
    • López-Hernández, E. & Serrano, L. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2. Folding & Design 1, 43-55 (1996).
    • (1996) Folding & Design , vol.1 , pp. 43-55
    • López-Hernández, E.1    Serrano, L.2
  • 37
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A. R., Serrano, L. & Wilmanns, M. Different folding transition states may result in the same native structure. Nature Struct. Biol. 3, 874-880 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 38
    • 0029893020 scopus 로고    scopus 로고
    • Analysis of the transition state in the unfolding of hen lysozyme by introduction of Gly-Pro and Pro-Gly sequences at the same site
    • Motoshima, H., Ueda, T. & Imoto, T. Analysis of the transition state in the unfolding of hen lysozyme by introduction of Gly-Pro and Pro-Gly sequences at the same site. J. Biochem. Tokyo 119, 1019-1023 (1996).
    • (1996) J. Biochem. Tokyo , vol.119 , pp. 1019-1023
    • Motoshima, H.1    Ueda, T.2    Imoto, T.3
  • 39
    • 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. 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).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 40
    • 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. 5, 79-84 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 41
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M. & Sali, A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5, 58-73 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 42
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhanovich, E. I. Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7, 29-40 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhanovich, E.I.1
  • 43
    • 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. 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).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 44
    • 0029015319 scopus 로고
    • The nature of the initial step in the conformational folding of disulphide-intact ribonuclease A
    • Houry, W. A., Rothwarf, D. M. & Scheraga, H. A. The nature of the initial step in the conformational folding of disulphide-intact ribonuclease A. Nature Struct. Biol. 2, 495-503 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 495-503
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 45
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G. & Kiefhaber, T. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270, 294-304 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 46
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models of protein folding kinetics
    • Zwanzig, R. W. Two-state models of protein folding kinetics. Proc. Natl. Acad. Sci. USA 94, 148-150 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 148-150
    • Zwanzig, R.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.