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Volumn 3, Issue 10, 1996, Pages 874-880

Different folding transition states may result in the same native structure

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; REVIEW;

EID: 0029760326     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1096-874     Document Type: Review
Times cited : (212)

References (31)
  • 1
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition
    • Jackson, S.E. & Fersht, A.R. Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition. Biochemistry 30, 10428-10435 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 2
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptoccocal protein G
    • Alexander, P., Ornan, J. & Bryan, P. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptoccocal protein G. Biochemistry 31, 7243-7248 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Ornan, J.2    Bryan, P.3
  • 4
    • 0028788480 scopus 로고
    • Evidence for a two state transition in the folding process of the activation domain of human procarboxipeptidase A2
    • Villegas, V. et al. Evidence for a two state transition in the folding process of the activation domain of human procarboxipeptidase A2. Biochemistry 34, 15105-15110 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1
  • 5
  • 6
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state transition
    • Viguera, A.R., Martinez, J.C., Filimonov, V.V., Mateo, P.L. & Serrano, L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state transition. Biochemistry 33, 2142-2150 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 7
    • 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
  • 8
    • 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., Otzen, 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    Otzen, D.E.2    Fersht, A.R.3
  • 9
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. Are there pathways for protein folding? J. Chim. Phys., 65, 44-45 (1968).
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 10
    • 0027432676 scopus 로고
    • Secondary structure of globular proteins at the early and the final stages in protein folding
    • Kuwajima, K., Semisotnov, G.V., Finkelstein, A.V. Sugai, S. & Ptitsyn, O.B. Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS. Lett. 3, 265-268 (1993).
    • (1993) FEBS. Lett. , vol.3 , pp. 265-268
    • Kuwajima, K.1    Semisotnov, G.V.2    Finkelstein, A.V.3    Sugai, S.4    Ptitsyn, O.B.5
  • 13
    • 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. 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).
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 14
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati, V. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallogr. 5, 802-810 (1952).
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 15
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio, A., Saraste, M. & Wilmanns, M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nature Struct. Biol. 1, 546-551 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 16
    • 0027948175 scopus 로고
    • Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implication for the mechanism of protein folding
    • Otzen, D.E., Itzhaki, L.S., Elmasry, N.F., Jackson, S.E. & Fersht, A .R. Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implication for the mechanism of protein folding Proc. Natl. Acad. Sci. USA 91, 10422-10425 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    Elmasry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 17
    • 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
  • 18
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI2
    • López-Hernández, E. & Serrano, L. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI2. Folding & Design 1, 43-55 (1996).
    • (1996) Folding & Design , vol.1 , pp. 43-55
    • López-Hernández, E.1    Serrano, L.2
  • 19
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A.R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA 92, 10869-10873 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 20
    • 0343059020 scopus 로고    scopus 로고
    • Conformational analysis of peptides corresponding to β-hairpins and a β-sheet that represent the entire sequence of the α-spectrin SH3 domain
    • Viguera, A.R., Jiménez, M.A., Rico, M. & Serrano, L. Conformational analysis of peptides corresponding to β-hairpins and a β-sheet that represent the entire sequence of the α-spectrin SH3 domain. J. Mol. Biol. 255, 507-521 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 507-521
    • Viguera, A.R.1    Jiménez, M.A.2    Rico, M.3    Serrano, L.4
  • 21
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., Abkevich, V. & Ptitsyn, O. Conserved residues and the mechanism of protein folding. Nature 379, 96-98 (1996).
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 22
    • 0001756859 scopus 로고
    • Is there a single pathway for the folding of a polypeptide chain?
    • Harrison, S.C. & Durbin, R. Is there a single pathway for the folding of a polypeptide chain?. Proc. Natl. Acad. Sci. USA 82, 4028-4030 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4028-4030
    • Harrison, S.C.1    Durbin, R.2
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: An automated package for molecular replacement. Acta Crystallogr. A50, 157-163 (1994).
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
  • 26
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. Automated refinement of protein models. Acta Crystallogr. D49, 129-147 (1993).
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 27
    • 2642699794 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotypic selection
    • Kunkel, T.A. Rapid and efficient site-directed mutagenesis without phenotypic selection. Proc. natn. Acad. Sci. U.S.A. 82, 488-492 (1985).
    • (1985) Proc. Natn. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 28
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with a modified T7 lac promoter for expression of proteins in Escherichia coli
    • Peränen, J., Rikkonen, M., Hyvönen, M. & Kääriäinen, L. T7 vectors with a modified T7 lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236, 371-373 (1996).
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peränen, J.1    Rikkonen, M.2    Hyvönen, M.3    Kääriäinen, L.4
  • 29
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure reactivity relationships and engineered proteins: Observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding of barnase
    • Matthews, J. M. & Fersht, A.R. Exploring the energy surface of protein folding by structure reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding of barnase. Biochemistry 34, 6805-4814 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6805-14814
    • Matthews, J.M.1    Fersht, A.R.2
  • 30
    • 0025398721 scopus 로고
    • WHAT if - A molecular modeling and drug design program
    • Vriend, G. WHAT IF - a molecular modeling and drug design program. J. Mol Graph. 8, 52-56 (1990).
    • (1990) J. Mol Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 31
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. Ribbons 2.0. J. Appl. Cryst. 24, 958-961 (1991).
    • (1991) J. Appl. Cryst. , vol.24 , pp. 958-961
    • Carson, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.