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Volumn 94, Issue 12, 2008, Pages 4828-4836

Global and local structural changes of cytochrome c and lysozyme characterized by a multigroup unfolding process

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; LYSOZYME;

EID: 45849135628     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.124214     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A., and H. S. Chan. 1997. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 2
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. 2001. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond., B. Biol. Sci. 356:133-145.
    • (2001) Philos. Trans. R. Soc. Lond., B. Biol. Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 3
    • 0035354585 scopus 로고    scopus 로고
    • Changes in biomolecular conformation seen by small angle x-ray scattering
    • Doniach, S. 2001. Changes in biomolecular conformation seen by small angle x-ray scattering. Chem. Rev. 101:1763-1778.
    • (2001) Chem. Rev , vol.101 , pp. 1763-1778
    • Doniach, S.1
  • 4
    • 0030745849 scopus 로고    scopus 로고
    • Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme
    • Ibarra-Molero, B., and J. M. Sanchez-Ruiz. 1997. Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme. Biochemistry. 36:9616-9624.
    • (1997) Biochemistry , vol.36 , pp. 9616-9624
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 5
    • 1842531459 scopus 로고    scopus 로고
    • Cytochrome c folding dynamics
    • Wrinkler, J. R. 2004. Cytochrome c folding dynamics. Curr. Opin. Chem. Biol. 8:169-174.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 169-174
    • Wrinkler, J.R.1
  • 6
    • 4644359012 scopus 로고    scopus 로고
    • How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization
    • Maity, H., M. Maity, and S. W. Englander. 2004. How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization. J. Mol. Biol. 343:223-233.
    • (2004) J. Mol. Biol , vol.343 , pp. 223-233
    • Maity, H.1    Maity, M.2    Englander, S.W.3
  • 7
    • 0035193329 scopus 로고    scopus 로고
    • Structural characterization of the pH-denatured states of ferricytochrome-c by synchrotron small angle x-ray scattering
    • Cinelli, S., F. Spinozzi, R. Itri, S. Finet, F. Garsughi, G. Onori, and P. Mariani. 2001. Structural characterization of the pH-denatured states of ferricytochrome-c by synchrotron small angle x-ray scattering. Biophys. J. 81:3522-3533.
    • (2001) Biophys. J , vol.81 , pp. 3522-3533
    • Cinelli, S.1    Spinozzi, F.2    Itri, R.3    Finet, S.4    Garsughi, F.5    Onori, G.6    Mariani, P.7
  • 8
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch, M. H. J., P. Vachette, and D. I. Svergun. 2003. Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36:147-227.
    • (2003) Q. Rev. Biophys , vol.36 , pp. 147-227
    • Koch, M.H.J.1    Vachette, P.2    Svergun, D.I.3
  • 10
    • 28444453002 scopus 로고    scopus 로고
    • Refinement of multidomain protein structures by combination of solution small-angle x-ray scattering and NMR data
    • Grishaev, A., J. Wu, J. Trewhella, and A. Bax. 2005. Refinement of multidomain protein structures by combination of solution small-angle x-ray scattering and NMR data. J. Am. Chem. Soc. 127:16621-16628.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16621-16628
    • Grishaev, A.1    Wu, J.2    Trewhella, J.3    Bax, A.4
  • 12
    • 33847306593 scopus 로고    scopus 로고
    • A unified mechanism for protein folding: Predetermined pathways with optional errors
    • Krishna, M. M. G., and S. W. Englander. 2007. A unified mechanism for protein folding: predetermined pathways with optional errors. Protein Sci. 16:449-464.
    • (2007) Protein Sci , vol.16 , pp. 449-464
    • Krishna, M.M.G.1    Englander, S.W.2
  • 15
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Shakhnovich, E. I. 1994. Proteins with selected sequences fold into unique native conformation. Phys. Rev. Lett. 72:3907-3910.
    • (1994) Phys. Rev. Lett , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 16
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V. I., A. M. Gutin, and E. I. Shakhnovich. 1995. Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 252:460-471.
    • (1995) J. Mol. Biol , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 17
    • 0037166875 scopus 로고    scopus 로고
    • Exact solution of the Muñoz-Eaton model for protein folding
    • Bruscolini, P., and A. Pelizzola. 2002. Exact solution of the Muñoz-Eaton model for protein folding. Phys. Rev. Lett. 88:258101-258104.
    • (2002) Phys. Rev. Lett , vol.88 , pp. 258101-258104
    • Bruscolini, P.1    Pelizzola, A.2
  • 18
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Muñoz, V., P. A. Thompson, J. Hofrichter, and W. A. Eaton. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature. 390:196-200.
    • (1997) Nature , vol.390 , pp. 196-200
    • Muñoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 19
    • 0038813543 scopus 로고    scopus 로고
    • One-dimensional Ising model applied to protein folding
    • Bakk, A., and J. S. Hoye. 2003. One-dimensional Ising model applied to protein folding. Physica A. 323:504-518.
    • (2003) Physica A , vol.323 , pp. 504-518
    • Bakk, A.1    Hoye, J.S.2
  • 20
    • 33746075741 scopus 로고    scopus 로고
    • Application of the generalized kinetic Ising model to the kinetics of protein folding
    • Liang, K. K., M. Hayashi, Y. J. Shiu, Y. Mo, J. Shao, J. Yan, and S. H. Lin. 2003. Application of the generalized kinetic Ising model to the kinetics of protein folding. J. Chin. Chem. Soc. 50:335-338.
    • (2003) J. Chin. Chem. Soc , vol.50 , pp. 335-338
    • Liang, K.K.1    Hayashi, M.2    Shiu, Y.J.3    Mo, Y.4    Shao, J.5    Yan, J.6    Lin, S.H.7
  • 22
    • 34248327297 scopus 로고    scopus 로고
    • A modified Ising model for the thermodynamic properties of local and global protein folding-unfolding observed by circular dichroism and small angle x-ray scattering
    • Shiu, Y. J., U. Jeng, C. Su, Y.-S. Huang, M. Hayashi, K.-K. Liang, Y.-L. Yeh, and S.-H. Lin. 2007. A modified Ising model for the thermodynamic properties of local and global protein folding-unfolding observed by circular dichroism and small angle x-ray scattering. J. Appl. Cryst. 40:s195-s199.
    • (2007) J. Appl. Cryst , vol.40
    • Shiu, Y.J.1    Jeng, U.2    Su, C.3    Huang, Y.-S.4    Hayashi, M.5    Liang, K.-K.6    Yeh, Y.-L.7    Lin, S.-H.8
  • 24
    • 85031358274 scopus 로고    scopus 로고
    • Yeh, Y. L., K. K. Liang, C. H. Chang, Y. J. Shiu, C. Su, M. Hayashi, G. Yang, J. M. Yuan, C. L. Chyan, S. Jang, F. Y. Li, and S. H. Lin. 2004. Physical chemistry of protein folding - experiments and theories. Trends in Phys. Chem. 40:169-205.
    • Yeh, Y. L., K. K. Liang, C. H. Chang, Y. J. Shiu, C. Su, M. Hayashi, G. Yang, J. M. Yuan, C. L. Chyan, S. Jang, F. Y. Li, and S. H. Lin. 2004. Physical chemistry of protein folding - experiments and theories. Trends in Phys. Chem. 40:169-205.
  • 28
    • 34248398037 scopus 로고    scopus 로고
    • Charge interaction and temperature effects on the solution structure of lysozyme as revealed by small-angle x-ray scattering
    • Huang, Y.-S., U. Jeng, Y. J. Shiu, Y.-H. Lai, and Y.-S. Sun. 2007. Charge interaction and temperature effects on the solution structure of lysozyme as revealed by small-angle x-ray scattering. J. Appl. Cryst. 40:s165-s169.
    • (2007) J. Appl. Cryst , vol.40
    • Huang, Y.-S.1    Jeng, U.2    Shiu, Y.J.3    Lai, Y.-H.4    Sun, Y.-S.5
  • 29
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun, D. I., M. V. Petoukhov, and M. H. J. Koch. 2001. Determination of domain structure of proteins from x-ray solution scattering. Biophys. J. 80:2946-2953.
    • (2001) Biophys. J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 30
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:482-501.
    • (1994) Biophys. J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 31
    • 85031354655 scopus 로고    scopus 로고
    • MacroModel, version 9.1. 2007. Schrödinger, New York
    • MacroModel, version 9.1. 2007. Schrödinger, New York.
  • 32
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still, W. C., A. Tempczyk, R. C. Hawley, and T. Hendrickson. 1990. Semianalytical treatment of solvation for molecular mechanics and dynamics. J. Am. Chem. Soc. 112:6127-6129.
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 35
    • 0038635898 scopus 로고    scopus 로고
    • Microsecond structural fluctuations in denatured cytochrome c and the mechanism of rapid chain contraction
    • Rischel, C., L. E. Jørgensen, and Z. Foldes-Papp. 2003. Microsecond structural fluctuations in denatured cytochrome c and the mechanism of rapid chain contraction. J. Phys. Condens. Matter. 15:S1725-S1735.
    • (2003) J. Phys. Condens. Matter , vol.15
    • Rischel, C.1    Jørgensen, L.E.2    Foldes-Papp, Z.3
  • 36
    • 0041812990 scopus 로고    scopus 로고
    • Effect of polyglutamate on the thermal stability of ferricytochrome c
    • Bágel'ová, J., M. Antalík, and Z. Tomori. 1997. Effect of polyglutamate on the thermal stability of ferricytochrome c. Biochem. Mol. Biol. Int. 43:891-900.
    • (1997) Biochem. Mol. Biol. Int , vol.43 , pp. 891-900
    • Bágel'ová, J.1    Antalík, M.2    Tomori, Z.3
  • 37
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c, effects of acetylation, heat, urea and guanidine-hydrochloride
    • Hagihara, Y., Y. Tan, and Y. Goto. 1994. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c, effects of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol. 237:336-348.
    • (1994) J. Mol. Biol , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3
  • 38
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., T. R. Sosnick, L. Mayne, and S. W. Englander. 1995. Protein folding intermediates: native-state hydrogen exchange. Science. 169:192-197.
    • (1995) Science , vol.169 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 40
    • 0030572626 scopus 로고    scopus 로고
    • A lysozyme folding intermediate revealed by solution x-ray scattering
    • Chen, L., K. O. Hodgson, and S. Doniach. 1996. A lysozyme folding intermediate revealed by solution x-ray scattering. J. Mol. Biol. 261:658-671.
    • (1996) J. Mol. Biol , vol.261 , pp. 658-671
    • Chen, L.1    Hodgson, K.O.2    Doniach, S.3
  • 42
    • 0037306725 scopus 로고    scopus 로고
    • Competitive model on denaturant-mediated protein unfolding
    • Murugan, R. 2003. Competitive model on denaturant-mediated protein unfolding. Biophys. J. 84:770-774.
    • (2003) Biophys. J , vol.84 , pp. 770-774
    • Murugan, R.1
  • 43
    • 0032995379 scopus 로고    scopus 로고
    • Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle x-ray scattering
    • Arai, S., and M. Hirai. 1999. Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle x-ray scattering. Biophys. J. 76:2192-2197.
    • (1999) Biophys. J , vol.76 , pp. 2192-2197
    • Arai, S.1    Hirai, M.2
  • 44
    • 0007290991 scopus 로고
    • SANS studies of concentrated protein solutions: Determination of the charge, hydration, and H/D exchange in cytochrome c
    • Wu, C. F., and S. H. Chen. 1987. SANS studies of concentrated protein solutions: determination of the charge, hydration, and H/D exchange in cytochrome c. J. Chem. Phys. 87:6199-6205.
    • (1987) J. Chem. Phys , vol.87 , pp. 6199-6205
    • Wu, C.F.1    Chen, S.H.2


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