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Volumn 276, Issue 2, 1998, Pages 505-515

Thermodynamic stability and folding of GroEL minichaperones

Author keywords

Apical domain; Chaperone; Kinetics; Minichaperone; Protein folding

Indexed keywords

CHAPERONIN; DYE;

EID: 0032548994     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1538     Document Type: Article
Times cited : (43)

References (31)
  • 2
    • 0024291318 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method 2. Incorporation of Δg N-U values in a thermodynamic cycle
    • Bolen D.W., Santoro M.M. Unfolding free energy changes determined by the linear extrapolation method 2. Incorporation of ΔG N-U values in a thermodynamic cycle. Biochemistry. 27:1988;8069-8074
    • (1988) Biochemistry , vol.27 , pp. 8069-8074
    • Bolen, D.W.1    Santoro, M.M.2
  • 4
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K., Adams P.D., Brünger A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2:1995;1083-1094
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 5
    • 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
  • 6
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • Buckle A.M., Zahn R., Fersht A.R. A structural model for GroEL-polypeptide recognition. Proc. Natl Acad. Sci. USA. 94:1997;3571-3575
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 7
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J., Fersht A.R. Engineered disulfide bonds as probes of the folding pathway of barnase increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:1993;4322-4329
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 8
    • 0142229698 scopus 로고    scopus 로고
    • MSTARA and MSTARI: Interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data
    • Cölfen H., Harding S.E. MSTARA and MSTARI Interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data. Eur. Biophys. J. 25:1997;333-346
    • (1997) Eur. Biophys. J. , vol.25 , pp. 333-346
    • Cölfen, H.1    Harding, S.E.2
  • 9
    • 0004243192 scopus 로고
    • Berlin, Heidelberg, NewYork, London, Paris, Tokyo: Springer-Verlag
    • Demchenko A. Ultraviolet Spectroscopy of Proteins. 1986;Springer-Verlag, Berlin, Heidelberg, NewYork, London, Paris, Tokyo
    • (1986) Ultraviolet Spectroscopy of Proteins
    • Demchenko, A.1
  • 10
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn
    • Dyson H.J., Rance M., Houghten R.A., Lerner R.A., Wright P.E. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 201:1988;161-200
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 11
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys.J. 66:1994;482-501
    • (1994) Biophys.J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 12
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet O., Ziegelhoffer T., Georgopoulos C. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1989;1379-1385
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 13
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton W.A., Horwich A.L. GroEL-mediated protein folding. Protein Sci. 6:1997;743-760
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 14
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • Fersht A.R. Protein folding and stability the pathway of folding of barnase. FEBS Letters. 325:1993;5-16
    • (1993) FEBS Letters , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 15
    • 0008221693 scopus 로고
    • The Optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system
    • S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge: Royal Soc. Chem
    • Giebeler R. The Optima XL-A A new analytical ultracentrifuge with a novel precision absorption optical system. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;16-25 Royal Soc. Chem, Cambridge
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 16-25
    • Giebeler, R.1
  • 16
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 17
    • 0028841921 scopus 로고
    • Residual structure in urea-denatured chaperonin GroEL
    • Gorovits B.M., Seale J.W., Horowitz P.M. Residual structure in urea-denatured chaperonin GroEL. Biochemistry. 34:1995;13928-13933
    • (1995) Biochemistry , vol.34 , pp. 13928-13933
    • Gorovits, B.M.1    Seale, J.W.2    Horowitz, P.M.3
  • 18
    • 33947343329 scopus 로고
    • The preparation of acetate and phosphate buffer solutions of known pH and ionic strength
    • Green A.A. The preparation of acetate and phosphate buffer solutions of known pH and ionic strength. J. Am. Chem. Soc. 55:1933;2331
    • (1933) J. Am. Chem. Soc. , vol.55 , pp. 2331
    • Green, A.A.1
  • 19
    • 0027457691 scopus 로고
    • A comment on: The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): Evidence for the presence of a single tryptophan, by N. C. Price, S. M. Kelly, S. Wood and A. auf der Mauer (1991
    • Hayer-Hartl M.K., Hartl F.-U. A comment on: The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan, by N. C. Price, S. M. Kelly, S. Wood and A. auf der Mauer (1991. FEBS Letters. 320:1993;83-84
    • (1993) FEBS Letters , vol.320 , pp. 83-84
    • Hayer-Hartl, M.K.1    Hartl, F.-U.2
  • 20
    • 0028000829 scopus 로고
    • Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein
    • Kim D., Kim C., Park C. Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein. J. Mol. Biol. 240:1994;385-395
    • (1994) J. Mol. Biol. , vol.240 , pp. 385-395
    • Kim, D.1    Kim, C.2    Park, C.3
  • 21
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek A., Kellis J.J., Serrano L., Bycroft M., Fersht A.R. Transient folding intermediates characterized by protein engineering. Nature. 346:1990;440-445
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis, J.J.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 22
    • 0028023363 scopus 로고
    • Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding
    • Mendoza J.A., Demeler B., Horowitz P.M. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. J. Biol. Chem. 269:1994;2447-2451
    • (1994) J. Biol. Chem. , vol.269 , pp. 2447-2451
    • Mendoza, J.A.1    Demeler, B.2    Horowitz, P.M.3
  • 24
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 25
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single-domain proteins
    • T.E. Creighton. New York: W. H. Freeman and Company
    • Schmid F.X. Kinetics of unfolding and refolding of single-domain proteins. Creighton T.E. Protein Folding. 1992;197-241 W. H. Freeman and Company, New York
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 27
    • 0029142612 scopus 로고
    • Refolding and reassembly of active chaperonin GroEL after denaturation
    • Ybarra J., Horowitz P.M. Refolding and reassembly of active chaperonin GroEL after denaturation. J. Biol. Chem. 270:1995;22113-22115
    • (1995) J. Biol. Chem. , vol.270 , pp. 22113-22115
    • Ybarra, J.1    Horowitz, P.M.2
  • 29
    • 0030576536 scopus 로고    scopus 로고
    • Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
    • Zahn R., Perrett S., Fersht A.R. Conformational states bound by the molecular chaperones GroEL and SecB a hidden unfolding (annealing) activity. J. Mol. Biol. 261:1996;43-61
    • (1996) J. Mol. Biol. , vol.261 , pp. 43-61
    • Zahn, R.1    Perrett, S.2    Fersht, A.R.3
  • 30
    • 0028025404 scopus 로고
    • Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase
    • Zahn R., Plückthun A. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase. J. Mol. Biol. 242:1994;165-174
    • (1994) J. Mol. Biol. , vol.242 , pp. 165-174
    • Zahn, R.1    Plückthun, A.2
  • 31
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn R., Perrett S., Stenberg G., Fersht A.R. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996;642-645
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.