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Volumn 291, Issue 2, 1999, Pages 429-444

Folding pathway of FKBP12 and characterisation of the transition state

Author keywords

FKBP12; Immunophilin; Protein folding; Transition state; Two state folding

Indexed keywords

IMMUNOPHILIN; TRIFLUOROETHANOL;

EID: 0032799756     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2941     Document Type: Article
Times cited : (94)

References (54)
  • 1
    • 84996108580 scopus 로고
    • Estimation of the stability of globular-proteins
    • Ahmad F., Bigelow C. C. Estimation of the stability of globular-proteins. Biopolymers. 25:1986;1623-1633.
    • (1986) Biopolymers , vol.25 , pp. 1623-1633
    • Ahmad, F.1    Bigelow, C.C.2
  • 2
    • 0025647885 scopus 로고
    • Two distinct signal transmission pathways in lymphocytes-T cells are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin
    • Bierer B. E., Mattila P. S., Standaert R. F., Herzenberg L. A., Burakoff S. J., Crabtree G., Schreiber S. L. Two distinct signal transmission pathways in lymphocytes-T cells are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin. Proc. Natl Acad. Sci. USA. 87:1990;9231-9235.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9231-9235
    • Bierer, B.E.1    Mattila, P.S.2    Standaert, R.F.3    Herzenberg, L.A.4    Burakoff, S.J.5    Crabtree, G.6    Schreiber, S.L.7
  • 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., Halvorson H. R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry. 14:1975;4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 5
    • 0030567341 scopus 로고    scopus 로고
    • Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol
    • CammersGoodwin A., Allen T. J., Oslick S. L., Mcclure K. F., Lee J. H., Kemp D. S. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 118:1996;3082-3090.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3082-3090
    • Cammersgoodwin, A.1    Allen, T.J.2    Oslick, S.L.3    Mcclure, K.F.4    Lee, J.H.5    Kemp, D.S.6
  • 7
    • 0024977347 scopus 로고
    • Low temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen B., Baase W. A., Schellman J. A. Low temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry. 26:1989;691-699.
    • (1989) Biochemistry , vol.26 , pp. 691-699
    • Chen, B.1    Baase, W.A.2    Schellman, J.A.3
  • 10
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition-state for folding of a protein-derived from experiment and simulation
    • Daggett V., Li A. J., Itzhaki L. S., Otzen D. E., Fersht A. R. Structure of the transition-state for folding of a protein-derived from experiment and simulation. J. Mol. Biol. 257:1996;430-440.
    • (1996) J. Mol. Biol. , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.J.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 11
    • 0032539209 scopus 로고    scopus 로고
    • A combined molecular dynamics and φ-value analysis of structure-reactivity relationships in the transition state and unfolding pathway of barnase: The structural basis of Hammond and anti-Hammond effects
    • Daggett V., Li A., Fersht A. R. A combined molecular dynamics and φ-value analysis of structure-reactivity relationships in the transition state and unfolding pathway of barnase: the structural basis of Hammond and anti-Hammond effects. J. Am. Chem. Soc. 120:1998;12740-12754.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12740-12754
    • Daggett, V.1    Li, A.2    Fersht, A.R.3
  • 13
    • 0028082357 scopus 로고
    • Probing the structure of folding intermediates
    • Evans P. A., Radford S. E. Probing the structure of folding intermediates. Curr. Opin. Struct. Biol. 4:1994;100-106.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 100-106
    • Evans, P.A.1    Radford, S.E.2
  • 14
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-collapse mechanism for the folding of chymotrypsin inhibitor 2 (CI2) and its consequences
    • Fersht A. R. Optimization of rates of protein folding: the nucleation-collapse mechanism for the folding of chymotrypsin inhibitor 2 (CI2) and its consequences. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 15
    • 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. The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224:1992;771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 16
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for folding/unfolding of FKBP12
    • ???; ???-???
    • Fulton K. F., Main E. R. G., Daggett V., Jackson S. E. Mapping the interactions present in the transition state for folding/unfolding of FKBP12. J. Mol. Biol. ??? 1999; ???-???
    • (1999) J. Mol. Biol.
    • Fulton, K.F.1    Main, E.R.G.2    Daggett, V.3    Jackson, S.E.4
  • 17
    • 84985715908 scopus 로고
    • NMR-studies of the rates of proline cis-trans isomerization in oligopeptides
    • Grathwohl C., Wuthrich K. NMR-studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers. 20:1981;2623-2633.
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wuthrich, K.2
  • 18
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S. E. How do small single-domain proteins fold? Fold. Design. 3:1998;R81-R90.
    • (1998) Fold. Design , vol.3
    • Jackson, S.E.1
  • 19
    • 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. 30:1991a;10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 20
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor-2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry. 30:1991b;10436-10443.
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 21
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor-2
    • Jackson S. E., Moracci M., El Masry N., Johnson C. M., Fersht A. R. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor-2. Biochemistry. 32:1993;11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    El Masry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 22
    • 0029867394 scopus 로고    scopus 로고
    • Structure-function relationships in the FK506-binding protein (FKBP) family of peptidyl prolyl isomerases
    • Kay J. E. Structure-function relationships in the FK506-binding protein (FKBP) family of peptidyl prolyl isomerases. Biochem. J. 314:1996;361-385.
    • (1996) Biochem. J. , vol.314 , pp. 361-385
    • Kay, J.E.1
  • 23
    • 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. 3:1996;193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 24
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P. S., Baldwin R. L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:1982;459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 26
    • 0032555115 scopus 로고    scopus 로고
    • Synergy between simulation and experiment in describing the energy landscape of protein folding
    • Ladurner A. G., Itzhaki L. S., Daggett V., Fersht A. R. Synergy between simulation and experiment in describing the energy landscape of protein folding. Proc. Natl Acad. Sci. USA. 95:1998;8473-8478.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8473-8478
    • Ladurner, A.G.1    Itzhaki, L.S.2    Daggett, V.3    Fersht, A.R.4
  • 27
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding? J. Chim. Phys. 85:1968;44-45.
    • (1968) J. Chim. Phys. , vol.85 , pp. 44-45
    • Levinthal, C.1
  • 28
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition-state of chymotrypsin inhibitor 2 by molecular-dynamics simulations
    • Li A. J., Daggett V. Identification and characterization of the unfolding transition-state of chymotrypsin inhibitor 2 by molecular-dynamics simulations. J. Mol. Biol. 257:1996;412-429.
    • (1996) J. Mol. Biol. , vol.257 , pp. 412-429
    • Li, A.J.1    Daggett, V.2
  • 29
    • 0028297302 scopus 로고
    • Structural characterization of the FK506 binding-protein unfolded in urea and guanidine-hydrochloride
    • Logan T., Theriault Y., Fesik S. Structural characterization of the FK506 binding-protein unfolded in urea and guanidine-hydrochloride. J. Mol. Biol. 236:1994;637-648.
    • (1994) J. Mol. Biol. , vol.236 , pp. 637-648
    • Logan, T.1    Theriault, Y.2    Fesik, S.3
  • 30
    • 0031575421 scopus 로고    scopus 로고
    • Acceleration of the folding of hen lysozyme by trifluoroethanol
    • Lu H., Buck M., Radford S. E., Dobson C. M. Acceleration of the folding of hen lysozyme by trifluoroethanol. J. Mol. Biol. 265:1997;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
  • 31
    • 0032574698 scopus 로고    scopus 로고
    • "stability of FKBP12: The Context-dependent Nature of Destabilising Mutations"
    • Main E. R. G., Fulton K. F. G., Jackson S. E. "Stability of FKBP12: The Context-dependent Nature of Destabilising Mutations" Biochemistry. 37:1998;6145-6153.
    • (1998) Biochemistry , vol.37 , pp. 6145-6153
    • Main, E.R.G.1    Fulton, K.F.G.2    Jackson, S.E.3
  • 32
    • 0032879754 scopus 로고    scopus 로고
    • Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states?
    • Main E. R. G., Jackson S. E. Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states? Nature Struct. Biol. in the press:1999.
    • (1999) Nature Struct. Biol.
    • Main, E.R.G.1    Jackson, S.E.2
  • 33
    • 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. 90:1993;7814-7818.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 36
    • 0028057108 scopus 로고
    • Raster3D version 2.0-a program for photorealistic molecular graphics
    • Merritt E. A., Murphy M. E. P. Raster3D version 2.0-a program for photorealistic molecular graphics. Acta Crystallog. Sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 37
    • 0025826966 scopus 로고
    • Aolution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
    • Michnick S. W., Rosen M. K., Wandless T. J., Karplus M., Schreiber S. L. Aolution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science. 252:1991;836-842.
    • (1991) Science , vol.252 , pp. 836-842
    • Michnick, S.W.1    Rosen, M.K.2    Wandless, T.J.3    Karplus, M.4    Schreiber, S.L.5
  • 39
    • 0029738546 scopus 로고    scopus 로고
    • Induction of α-helix in the β-sheet protein tumor necrosis factor-α: Acid-induced denaturation
    • Narhi L. O., Philo J. S., Li T. S., Zhang M., Samal B., Arakawa T. Induction of α-helix in the β-sheet protein tumor necrosis factor-α: Acid-induced denaturation. Biochemistry. 35:1996;11454-11460.
    • (1996) Biochemistry , vol.35 , pp. 11454-11460
    • Narhi, L.O.1    Philo, J.S.2    Li, T.S.3    Zhang, M.4    Samal, B.5    Arakawa, T.6
  • 40
    • 0024473893 scopus 로고
    • Persistence of the α-helix stop signal in the S-peptide in TFE Solutions
    • Nelson J. W., Kallenbach N. R. Persistence of the α-helix stop signal in the S-peptide in TFE Solutions. Biochemistry. 28:1989;5256-5261.
    • (1989) Biochemistry , vol.28 , pp. 5256-5261
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 41
    • 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. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 42
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson A. D., Murphy K. P. Protein structure and the energetics of protein stability. Chem. Rev. 97:1997;1251-1267.
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1267
    • Robertson, A.D.1    Murphy, K.P.2
  • 43
    • 0026007026 scopus 로고
    • Mapping transition states of protein unfolding by protein engineering of ligand-binding sites
    • Sancho J., Meiering E., Fersht A. R. Mapping transition states of protein unfolding by protein engineering of ligand-binding sites. J. Mol. Biol. 221:1991;1007-1014.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1007-1014
    • Sancho, J.1    Meiering, E.2    Fersht, A.R.3
  • 45
    • 0029827590 scopus 로고    scopus 로고
    • Catalyzed and assisted protein folding of ribonuclease T1
    • Schmid F. X., Frech C., Scholz C., Walter S. Catalyzed and assisted protein folding of ribonuclease T1. Biol. Chem. 377:1996;417-424.
    • (1996) Biol. Chem. , vol.377 , pp. 417-424
    • Schmid, F.X.1    Frech, C.2    Scholz, C.3    Walter, S.4
  • 47
    • 0027385015 scopus 로고
    • The refolding of cis-peptidylprolyl and trans-peptidylprolyl isomers of barstar
    • Schreiber G., Fersht A. R. The refolding of cis-peptidylprolyl and trans-peptidylprolyl isomers of barstar. Biochemistry. 32:1993;11195-11203.
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 48
    • 0030467150 scopus 로고    scopus 로고
    • Destabilisation of native tertiary structural interactions is linked to helix-induction by 2,2,2-trifluoroethanol in proteins
    • Sivaraman T., Kumar T. K. S., Yu C. Destabilisation of native tertiary structural interactions is linked to helix-induction by 2,2,2-trifluoroethanol in proteins. Int. J. Biol. Macromol. 19:1996;235-239.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 235-239
    • Sivaraman, T.1    Kumar, T.K.S.2    Yu, C.3
  • 49
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282.
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 50
    • 0014718113 scopus 로고
    • Protein folding. Part C
    • Tanford C. Protein folding. Part C. Advan. Protein Chem. 24:1970;1-95.
    • (1970) Advan. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 54
    • 0032572054 scopus 로고    scopus 로고
    • An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2-propanol
    • Walgers R., Lee T. C., CammersGoodwin A. An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2-propanol. J. Am. Chem. Soc. 120:1998;5073-5079.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5073-5079
    • Walgers, R.1    Lee, T.C.2    Cammersgoodwin, A.3


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