메뉴 건너뛰기




Volumn 19, Issue 15, 2000, Pages 3870-3875

Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell

Author keywords

Excluded volume; Ficoll; Hen lysozyme; Macromolecular crowding; Protein refolding kinetics

Indexed keywords

ALBUMIN; CELL PROTEIN; FICOLL; LYSOZYME;

EID: 0034254189     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.15.3870     Document Type: Article
Times cited : (244)

References (26)
  • 1
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R.L. (1995) The nature of protein folding pathways: the classical versus the new view. J. Biomol. NMR, 5, 103-109.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A. and Chan, H.S. (1997) From Levinthal to pathways to funnels. Nature Struct. Biol, 4, 10-19.
    • (1997) Nature Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 3
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson, C.M. and Karplus, M. (1999) The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol., 9, 92-101.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 4
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson, C.M., Evans, P.A. and Radford, S.E. (1994) Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci., 19, 31-37.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 5
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C.M., Sali, A. and Karplus, M. (1998) Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed., 37, 868-893.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 7
    • 0025843479 scopus 로고
    • Kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg-white lysozyme
    • Goldberg, M.E., Rudolph, R. and Jaenicke, R.A. (1991) Kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg-white lysozyme. Biochemistry, 30, 2790-2797.
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.A.3
  • 8
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han, J. and Herzfeld, J. (1993) Macromolecular diffusion in crowded solutions. Biophys. J., 65, 1155-1161.
    • (1993) Biophys. J. , vol.65 , pp. 1155-1161
    • Han, J.1    Herzfeld, J.2
  • 10
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells
    • Luby-Phelps, K., Castle, P.E., Lansing Taylor, D. and Lanni, F. (1987) Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proc. Natl Acad. Sci. USA, 84, 4910-4913.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Lansing Taylor, D.3    Lanni, F.4
  • 11
    • 0031030690 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on chaperonin-mediated protein folding
    • Martin, J. and Hartl, F.-U. (1997) The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc. Natl Acad. Sci. USA, 94, 1107-1112.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1107-1112
    • Martin, J.1    Hartl, F.-U.2
  • 12
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding: Insight into the roles of domains in the folding process
    • Matagne, A., Radford, S.E. and Dobson, C.M. (1997) Fast and slow tracks in lysozyme folding: insight into the roles of domains in the folding process. J. Mol. Biol., 267, 1068-1074.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 13
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • Minton, A.P. (1981) Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers, 20, 2093-2120.
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 14
    • 0034039755 scopus 로고    scopus 로고
    • Effect of a concentrated 'inert' macromolecule cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model
    • Minton, A.P. (2000a) Effect of a concentrated 'inert' macromolecule cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model. Biophys. J., 78, 101-109.
    • (2000) Biophys. J. , vol.78 , pp. 101-109
    • Minton, A.P.1
  • 15
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding on protein assembly
    • Minton, A.P. (2000b) Implications of macromolecular crowding on protein assembly. Curr. Opin. Struct. Biol., 10, 34-39.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 16
    • 0034628613 scopus 로고    scopus 로고
    • Protein folding: Thickening the broth
    • Minton, A.P. (2000c) Protein folding: thickening the broth. Curr. Biol., 10, R97-R99.
    • (2000) Curr. Biol. , vol.10
    • Minton, A.P.1
  • 17
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S.E., Dobson, C.M. and Evans, P.A. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature, 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 18
    • 0032079008 scopus 로고    scopus 로고
    • Biophysical compensation mechanisms buffering E.coli protein-nucleic acid interactions against changing environments
    • Record, M.T., Courtenay, D.S., Cayley, D.S. and Guttman, H.J. (1998) Biophysical compensation mechanisms buffering E.coli protein-nucleic acid interactions against changing environments. Trends Biochem. Sci., 23, 190-194.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 190-194
    • Record, M.T.1    Courtenay, D.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 19
    • 0033462152 scopus 로고    scopus 로고
    • Comparison of the kinetics of S-S bond, secondary structure and active site formation during refolding of reduced denatured hen egg white lysozyme
    • Roux, P., Ruoppolo, M, Chaffotte, A.-F. and Goldberg, M.E. (1999) Comparison of the kinetics of S-S bond, secondary structure and active site formation during refolding of reduced denatured hen egg white lysozyme. Protein Sci., 8, 2751-2760.
    • (1999) Protein Sci. , vol.8 , pp. 2751-2760
    • Roux, P.1    Ruoppolo, M.2    Chaffotte, A.-F.3    Goldberg, M.E.4
  • 20
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • Swaminathan, R., Hwang, C.P. and Verkman, A.S. (1997) Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J., 72, 1900-1907.
    • (1997) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hwang, C.P.2    Verkman, A.S.3
  • 21
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg, B., Ellis, R.J. and Dobson, C.M. (1999a) Effects of macromolecular crowding on protein folding and aggregation. EMBO J., 18, 6927-6933.
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 22
    • 0032765075 scopus 로고    scopus 로고
    • Characterisation of the dominant oxidative folding intermediate of hen lysozyme
    • van den Berg, B., Chung, E.W., Robinson, C.V. and Dobson, C.M. (1999b) Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J. Mol. Biol., 290, 781-796.
    • (1999) J. Mol. Biol. , vol.290 , pp. 781-796
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Dobson, C.M.4
  • 23
    • 0033199237 scopus 로고    scopus 로고
    • The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
    • van den Berg, B., Chung, E.W., Robinson, C.V., Mateo, P.L. and Dobson, C.M (1999c) The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J., 18, 4794-4803.
    • (1999) EMBO J. , vol.18 , pp. 4794-4803
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Mateo, P.L.4    Dobson, C.M.5
  • 24
    • 0025949415 scopus 로고
    • Re-examination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J.S. and Kim, P.S. (1991) Re-examination of the folding of BPTI: predominance of native intermediates. Science, 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 25
    • 0032762645 scopus 로고    scopus 로고
    • Crowding effects on EcoRV kinetics and binding
    • Wenner, J.R. and Bloomfield, V.A. (1999) Crowding effects on EcoRV kinetics and binding. Biophys. J., 77, 3234-3241.
    • (1999) Biophys. J. , vol.77 , pp. 3234-3241
    • Wenner, J.R.1    Bloomfield, V.A.2
  • 26
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical and physiological consequences
    • Zimmerman, S.B. and Minton, A.P. (1993) Macromolecular crowding: biochemical, biophysical and physiological consequences. Annu. Rev. Biophys. Biomol. Struct., 22, 27-75.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-75
    • Zimmerman, S.B.1    Minton, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.