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Volumn 10, Issue 8, 2003, Pages 658-662

Parallel protein-unfolding pathways revealed and mapped

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0043125488     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb947     Document Type: Article
Times cited : (152)

References (32)
  • 2
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C.M., Sali, A. & Karplus, M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37, 868-893 (1998).
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 3
    • 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. Biomol. NMR 5, 103-109 (1995).
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 4
    • 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
  • 5
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner, A.R., Sali, A., Smith, L.J., Dobson, C.M. & Karplus, M. Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci. 25, 331-339 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 6
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi, F.N., Nath, U. & Udgaonkar, J.B. Multiple intermediates and transition states during protein unfolding. Nat. Struct. Biol. 4, 1016-1023 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1016-1023
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 7
    • 0030735983 scopus 로고    scopus 로고
    • Competing unfolding pathways
    • Baldwin, R.L. Competing unfolding pathways. Nat. Struct. Biol. 4, 965-966 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 965-966
    • Baldwin, R.L.1
  • 8
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • Fowler, S.B. & Clarke, J. Mapping the folding pathway of an immunoglobulin domain: structural detail from phi value analysis and movement of the transition state. Structure 9, 355-366 (2001).
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 9
    • 0028856785 scopus 로고
    • Optimisation of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A.R. Optimisation of rates of protein folding: the nucleation-condensation mechanism and its implications. Biochemistry 92, 10869-10873 (1995).
    • (1995) Biochemistry , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 10
    • 0014364651 scopus 로고
    • Protein denaturation. B. The transition from native to denatured state
    • Tanford, C. Protein denaturation. B. The transition from native to denatured state. Adv. Protein Chem. 23, 218-282 (1968).
    • (1968) Adv. Protein Chem. , vol.23 , pp. 218-282
    • Tanford, C.1
  • 11
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding
    • Oliveberg, M., Tan, Y.-J., Silow, M. & Fersht, A.R. The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. J. Mol. Biol. 277, 933-943 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 933-943
    • Oliveberg, M.1    Tan, Y.-J.2    Silow, M.3    Fersht, A.R.4
  • 12
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond, G.S. A correlation of reaction rates. J. Am. Chem. Soc. 77, 334-338 (1955).
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 334-338
    • Hammond, G.S.1
  • 13
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matoushchek, 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
    • Matoushchek, A.1    Fersht, A.R.2
  • 14
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez, I.E. & Kiefhaber, T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325, 367-376 (2002).
    • (2002) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 15
    • 0033580679 scopus 로고    scopus 로고
    • Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots
    • Otzen, D.E., Kristensen, O., Proctor, M, & Oliveberg, M. Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots. Biochemistry 38, 6499-6511 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6499-6511
    • Otzen, D.E.1    Kristensen, O.2    Proctor, M.3    Oliveberg, M.4
  • 16
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure-reactivity relationships and engineering proteins: Observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase
    • Matthews, J.M. & Fersht, A.R. Exploring the energy surface of protein folding by structure-reactivity relationships and engineering proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. Biochemistry 34, 6805-6814 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 17
    • 0032584281 scopus 로고    scopus 로고
    • Movement of the intermediate and rate determining state of barnase on the energy landscape with changing temperature
    • Dalby, P.A., Oliveberg, M. & Fersht, A.R. Movement of the intermediate and rate determining state of barnase on the energy landscape with changing temperature. Biochemistry 37, 4674-4679 (1998).
    • (1998) Biochemistry , vol.37 , pp. 4674-4679
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 18
    • 0032539209 scopus 로고    scopus 로고
    • Combined molecular dynamics and Φ-value analysis of structure-reactivity relationships in the transition state and unfolding pathway of barnase: Structural basis of Hammond and anti-Hammond effects
    • Daggett, V., Li, A. & Fersht, A.R. Combined molecular dynamics and Φ-value analysis of structure-reactivity relationships in the transition state and unfolding pathway of barnase: structural basis of Hammond and anti-Hammond effects. J. Am. Chem. Soc. 120, 12740-12754 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12740-12754
    • Daggett, V.1    Li, A.2    Fersht, A.R.3
  • 19
    • 0036293485 scopus 로고    scopus 로고
    • Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state
    • Otzen, D.E. & Oliveberg, M. Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state. J. Mol. Biol. 317, 613-627 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 613-627
    • Otzen, D.E.1    Oliveberg, M.2
  • 20
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A.R., Itzhaki, L.S., ElMasry, N.F., Matthews, J.M. & Otzen, D.E. Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl. Acad. Sci. USA 91, 10426-10429 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    ElMasry, N.F.3    Matthews, J.M.4    Otzen, D.E.5
  • 22
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Prot. Chem. 24, 1-95 (1970).
    • (1970) Adv. Prot. Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 23
    • 0035997388 scopus 로고    scopus 로고
    • Mechanisms of fast protein folding
    • Myers, J. & Oas, T.G. Mechanisms of fast protein folding. Annu. Rev. Biochem. 71, 783-815 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 783-815
    • Myers, J.1    Oas, T.G.2
  • 24
    • 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
    • Sanchez, I.E. & Kiefhaber, T. 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).
    • (2003) J. Mol. Biol. , vol.327 , pp. 867-884
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 26
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin formation in protein G
    • McCallister, E.L., Alm, E. & Baker, D. Critical role of β-hairpin formation in protein G. Nat. Struct. Biol. 7, 669-673 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 27
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • Nauli, S., Kuhlman, B. & Baker, D. Computer-based redesign of a protein folding pathway. Nat. Struct. Biol. 8, 602-605 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 28
    • 0026511656 scopus 로고
    • The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., Matouschek, A. & Serrano, L. The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 29
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • Lindberg, M., Tangrot, J. & Oliveberg, M. Complete change of the protein folding transition state upon circular permutation. Nat. Struct. Biol. 9, 818-822 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 818-822
    • Lindberg, M.1    Tangrot, J.2    Oliveberg, M.3
  • 30
    • 0037159944 scopus 로고    scopus 로고
    • Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways
    • Davis, R., Dobson, C.M. & Vendruscolo, M. Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways. J. Chem. Phys. 117, 9510-9517 (2002).
    • (2002) J. Chem. Phys. , vol.117 , pp. 9510-9517
    • Davis, R.1    Dobson, C.M.2    Vendruscolo, M.3
  • 31
    • 0033616713 scopus 로고    scopus 로고
    • Mechanical and chemical unfolding of a single protein: A comparison
    • Carrion-Vasquez, M. et al. Mechanical and chemical unfolding of a single protein: a comparison. Proc. Natl. Acad. Sci. USA 96, 3694-3699 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3694-3699
    • Carrion-Vasquez, M.1
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950 (1991).
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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