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Volumn 402, Issue 3, 2010, Pages 610-617

Measuring "Unmeasurable" folding kinetics of proteins by single-molecule force spectroscopy

Author keywords

Atomic force microscopy; Folding kinetics; Irreversible denaturation; Protein folding; Single molecule force spectroscopy

Indexed keywords

ENDO 1,4 BETA XYLANASE;

EID: 77956893949     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.059     Document Type: Article
Times cited : (5)

References (34)
  • 1
    • 0033612542 scopus 로고    scopus 로고
    • Two-state irreversible thermal denaturation of muscle creatine kinase
    • Lyubarev A.E., Kurganov B.I., Orlov V.N., Zhou H.M. Two-state irreversible thermal denaturation of muscle creatine kinase. Biophys. Chem. 1999, 79:199-204.
    • (1999) Biophys. Chem. , vol.79 , pp. 199-204
    • Lyubarev, A.E.1    Kurganov, B.I.2    Orlov, V.N.3    Zhou, H.M.4
  • 2
    • 0031467295 scopus 로고    scopus 로고
    • Analysis of differential scanning calorimetry data for proteins-criteria of validity of one-step mechanism of irreversible protein denaturation
    • Kurganov B.I., Lyubarev A.E., Sanchez-Ruiz J.M., Shnyrov V.L. Analysis of differential scanning calorimetry data for proteins-criteria of validity of one-step mechanism of irreversible protein denaturation. Biophys. Chem. 1997, 69:125-135.
    • (1997) Biophys. Chem. , vol.69 , pp. 125-135
    • Kurganov, B.I.1    Lyubarev, A.E.2    Sanchez-Ruiz, J.M.3    Shnyrov, V.L.4
  • 3
    • 0024469173 scopus 로고
    • Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase
    • Violet M., Meunier J.C. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase. Biochem. J. 1989, 263:665-670.
    • (1989) Biochem. J. , vol.263 , pp. 665-670
    • Violet, M.1    Meunier, J.C.2
  • 4
    • 0031873691 scopus 로고    scopus 로고
    • Scan-rate dependence in protein calorimetry: the reversible transitions of Bacillus circulans xylanase and a disulfide-bridge mutant
    • Davoodi J., Wakarchuk W.W., Surewicz W.K., Carey P.R. Scan-rate dependence in protein calorimetry: the reversible transitions of Bacillus circulans xylanase and a disulfide-bridge mutant. Protein Sci. 1998, 7:1538-1544.
    • (1998) Protein Sci. , vol.7 , pp. 1538-1544
    • Davoodi, J.1    Wakarchuk, W.W.2    Surewicz, W.K.3    Carey, P.R.4
  • 5
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: folding aggregates, inclusion bodies and amyloid
    • Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 1998, 3:R9-23.
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 6
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • Carrotta R., Bauer R., Waninge R., Rischel C. Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci. 2001, 10:1312-1318.
    • (2001) Protein Sci. , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 7
    • 0031021542 scopus 로고    scopus 로고
    • Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
    • Speed M.A., Morshead T., Wang D.I., King J. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci. 1997, 6:99-108.
    • (1997) Protein Sci. , vol.6 , pp. 99-108
    • Speed, M.A.1    Morshead, T.2    Wang, D.I.3    King, J.4
  • 8
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition
    • Speed M.A., Wang D.I., King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat. Biotechnol. 1996, 14:1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.2    King, J.3
  • 9
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates
    • King J., Haase-Pettingell C., Robinson A.S., Speed M., Mitraki A. Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates. FASEB J. 1996, 10:57-66.
    • (1996) FASEB J. , vol.10 , pp. 57-66
    • King, J.1    Haase-Pettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 10
    • 0347694974 scopus 로고    scopus 로고
    • On the extended beta-conformation propensity of polypeptides at high temperature
    • Yang W.Y., Larios E., Gruebele M. On the extended beta-conformation propensity of polypeptides at high temperature. J. Am. Chem. Soc. 2003, 125:16220-16227.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16220-16227
    • Yang, W.Y.1    Larios, E.2    Gruebele, M.3
  • 11
    • 0031024424 scopus 로고    scopus 로고
    • Thermostability and irreversible activity loss of exoglucanase/xylanase Cex from Cellulomonas fimi
    • Nikolova P.V., Creagh A.L., Duff S.J., Haynes C.A. Thermostability and irreversible activity loss of exoglucanase/xylanase Cex from Cellulomonas fimi. Biochemistry 1997, 36:1381-1388.
    • (1997) Biochemistry , vol.36 , pp. 1381-1388
    • Nikolova, P.V.1    Creagh, A.L.2    Duff, S.J.3    Haynes, C.A.4
  • 12
    • 0026734152 scopus 로고
    • Stereoselective hydrolysis catalyzed by related beta-1,4-glucanases and beta-1,4-xylanases
    • Gebler J., Gilkes N.R., Claeyssens M., Wilson D.B., Beguin P., Wakarchuk W.W., et al. Stereoselective hydrolysis catalyzed by related beta-1,4-glucanases and beta-1,4-xylanases. J. Biol. Chem. 1992, 267:12559-12561.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12559-12561
    • Gebler, J.1    Gilkes, N.R.2    Claeyssens, M.3    Wilson, D.B.4    Beguin, P.5    Wakarchuk, W.W.6
  • 13
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • Sinnott M.L. Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev. 1990, 90:1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 14
    • 0029666454 scopus 로고    scopus 로고
    • The pK(a) of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a C-13-NMR study of Bacillus circulans xylanase
    • McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Korner M., Plesniak L.A., et al. The pK(a) of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a C-13-NMR study of Bacillus circulans xylanase. Biochemistry 1996, 35:9958-9966.
    • (1996) Biochemistry , vol.35 , pp. 9958-9966
    • McIntosh, L.P.1    Hand, G.2    Johnson, P.E.3    Joshi, M.D.4    Korner, M.5    Plesniak, L.A.6
  • 15
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • Joshi M.D., Sidhu G., Nielsen J.E., Brayer G.D., Withers S.G., McIntosh L.P. Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry 2001, 40:10115-10139.
    • (2001) Biochemistry , vol.40 , pp. 10115-10139
    • Joshi, M.D.1    Sidhu, G.2    Nielsen, J.E.3    Brayer, G.D.4    Withers, S.G.5    McIntosh, L.P.6
  • 16
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active-site residues of the Bacillus circulans xylanase
    • Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M. Mutational and crystallographic analyses of the active-site residues of the Bacillus circulans xylanase. Protein Sci. 1994, 3:467-475.
    • (1994) Protein Sci. , vol.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 17
    • 0031056260 scopus 로고    scopus 로고
    • Positioning the acid/base catalyst in a glycosidase: studies with Bacillus circulans xylanase
    • Lawson S.L., Wakarchuk W.W., Withers S.G. Positioning the acid/base catalyst in a glycosidase: studies with Bacillus circulans xylanase. Biochemistry 1997, 36:2257-2265.
    • (1997) Biochemistry , vol.36 , pp. 2257-2265
    • Lawson, S.L.1    Wakarchuk, W.W.2    Withers, S.G.3
  • 18
    • 0028244925 scopus 로고
    • Identification of glutamic acid 78 as the active-site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry
    • Miao S.C., Ziser L., Aebersold R., Withers S.G. Identification of glutamic acid 78 as the active-site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry. Biochemistry 1994, 33:7027-7032.
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.C.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 19
    • 0029759746 scopus 로고    scopus 로고
    • Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity
    • Lawson S.L., Wakarchuk W.W., Withers S.G. Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity. Biochemistry 1996, 35:10110-10118.
    • (1996) Biochemistry , vol.35 , pp. 10110-10118
    • Lawson, S.L.1    Wakarchuk, W.W.2    Withers, S.G.3
  • 20
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation
    • Chi E.Y., Krishnan S., Randolph T.W., Carpenter J.F. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 2003, 20:1325-1336.
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 21
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 1997, 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 23
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez J.M., Li H. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 2004, 303:1674-1678.
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 24
    • 21444445531 scopus 로고    scopus 로고
    • The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments
    • Schwaiger I., Schleicher M., Noegel A.A., Rief M. The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments. EMBO Rep. 2005, 6:46-51.
    • (2005) EMBO Rep. , vol.6 , pp. 46-51
    • Schwaiger, I.1    Schleicher, M.2    Noegel, A.A.3    Rief, M.4
  • 25
    • 38049103717 scopus 로고    scopus 로고
    • Tandem repeating modular proteins avoid aggregation in single molecule force spectroscopy experiments
    • Dougan L., Fernandez J.M. Tandem repeating modular proteins avoid aggregation in single molecule force spectroscopy experiments. J. Phys. Chem. A 2007, 111:12402-12408.
    • (2007) J. Phys. Chem. A , vol.111 , pp. 12402-12408
    • Dougan, L.1    Fernandez, J.M.2
  • 26
    • 31044449315 scopus 로고    scopus 로고
    • Nonmechanical protein can have significant mechanical stability
    • Cao Y., Lam C., Wang M., Li H. Nonmechanical protein can have significant mechanical stability. Angew. Chem., Int. Ed. Engl. 2006, 45:642-645.
    • (2006) Angew. Chem., Int. Ed. Engl. , vol.45 , pp. 642-645
    • Cao, Y.1    Lam, C.2    Wang, M.3    Li, H.4
  • 27
    • 33846666463 scopus 로고    scopus 로고
    • Polyprotein of GB1 is an ideal artificial elastomeric protein
    • Cao Y., Li H. Polyprotein of GB1 is an ideal artificial elastomeric protein. Nat. Mater. 2007, 6:109-114.
    • (2007) Nat. Mater. , vol.6 , pp. 109-114
    • Cao, Y.1    Li, H.2
  • 28
    • 0026785573 scopus 로고
    • Inactivation of a beta-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-alpha-d-glucopyranosyl-enzyme intermediate: a detailed investigation
    • Street I.P., Kempton J.B., Withers S.G. Inactivation of a beta-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-alpha-d-glucopyranosyl-enzyme intermediate: a detailed investigation. Biochemistry 1992, 31:9970-9978.
    • (1992) Biochemistry , vol.31 , pp. 9970-9978
    • Street, I.P.1    Kempton, J.B.2    Withers, S.G.3
  • 29
    • 11744311356 scopus 로고
    • Statistical mechanics of supercoiled DNA
    • Marko J.F., Siggia E.D. Statistical mechanics of supercoiled DNA. Phys. Rev. E 1995, 52:2912-2938.
    • (1995) Phys. Rev. E , vol.52 , pp. 2912-2938
    • Marko, J.F.1    Siggia, E.D.2
  • 30
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • Wright C.F., Teichmann S.A., Clarke J., Dobson C.M. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 2005, 438:878-881.
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 31
    • 38949139507 scopus 로고    scopus 로고
    • Conformational equilibria in monomeric alpha-synuclein at the single-molecule level
    • Sandal M., Valle F., Tessari I., Mammi S., Bergantino E., Musiani F., et al. Conformational equilibria in monomeric alpha-synuclein at the single-molecule level. PLoS Biol. 2008, 6:e6.
    • (2008) PLoS Biol. , vol.6
    • Sandal, M.1    Valle, F.2    Tessari, I.3    Mammi, S.4    Bergantino, E.5    Musiani, F.6
  • 32
    • 59649095836 scopus 로고    scopus 로고
    • Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers
    • Brucale M., Sandal M., Di Maio S., Rampioni A., Tessari I., Tosatto L., et al. Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers. ChemBioChem 2009, 10:176-183.
    • (2009) ChemBioChem , vol.10 , pp. 176-183
    • Brucale, M.1    Sandal, M.2    Di Maio, S.3    Rampioni, A.4    Tessari, I.5    Tosatto, L.6
  • 33
    • 0027617799 scopus 로고
    • Overexpression of the Bacillus subtilis and circulans xylanases in Escherichia coli
    • Sung W.L., Luk C.K., Zahab D.M., Wakarchuk W. Overexpression of the Bacillus subtilis and circulans xylanases in Escherichia coli. Protein Expr. Purif. 1993, 4:200-206.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 200-206
    • Sung, W.L.1    Luk, C.K.2    Zahab, D.M.3    Wakarchuk, W.4


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