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Volumn 294, Issue 2, 1999, Pages 579-586

Process of biosynthetic protein folding determines the rapid formation of native structure

Author keywords

Bacterial luciferase; Cotranslational folding; Folding pathway; Protein biosynthesis; Protein folding

Indexed keywords

LUCIFERASE; UREA;

EID: 0033607484     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3281     Document Type: Article
Times cited : (30)

References (21)
  • 1
    • 0027178317 scopus 로고
    • Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme
    • Baldwin T. O., Ziegler M. M., Chaffotte A. F., Goldberg M. E. Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme. J. Biol. Chem. 268:1993;10766-10772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10766-10772
    • Baldwin, T.O.1    Ziegler, M.M.2    Chaffotte, A.F.3    Goldberg, M.E.4
  • 2
    • 0028286471 scopus 로고
    • Kinetics versus thermodynamics in protein folding
    • Baker D., Agard D. Kinetics versus thermodynamics in protein folding. Biochemistry. 33:1994;7505-7509.
    • (1994) Biochemistry , vol.33 , pp. 7505-7509
    • Baker, D.1    Agard, D.2
  • 3
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM- A flexible, portable system
    • Barshop B. A., Wrenn R. F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM- a flexible, portable system. Anal. Biochem. 130:1983;134-145.
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 6
    • 0027451307 scopus 로고
    • Folding of subtilisin BPN′: Role of the pro-sequence
    • Eder J., Rheinnecker M., Fersht A. R. Folding of subtilisin BPN′: role of the pro-sequence. J. Mol. Biol. 233:1993;293-304.
    • (1993) J. Mol. Biol. , vol.233 , pp. 293-304
    • Eder, J.1    Rheinnecker, M.2    Fersht, A.R.3
  • 7
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov A. N., Baldwin T. O. Contribution of cotranslational folding to the rate of formation of native protein structure. Proc. Natl Acad. Sci. USA. 92:1995;1227-1231.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1227-1231
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 8
    • 0031574908 scopus 로고    scopus 로고
    • GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
    • Fedorov A. N., Baldwin T. O. GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J. Mol. Biol. 268:1997a;712-723.
    • (1997) J. Mol. Biol. , vol.268 , pp. 712-723
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 9
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov A. N., Baldwin T. O. Cotranslational protein folding. J. Biol. Chem. 272:1997b;32715-32718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 10
    • 0031939208 scopus 로고    scopus 로고
    • Protein folding and assembly in a cell-free expression system
    • Fedorov A. N., Baldwin T. O. Protein folding and assembly in a cell-free expression system. Methods Enzymol. 290:1998;1-17.
    • (1998) Methods Enzymol. , vol.290 , pp. 1-17
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 11
    • 0029664970 scopus 로고    scopus 로고
    • The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions
    • Fisher A. J., Thompson T. B., Thoden J. B., Baldwin T. O., Rayment I. The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271:1996;21956-21968.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21956-21968
    • Fisher, A.J.1    Thompson, T.B.2    Thoden, J.B.3    Baldwin, T.O.4    Rayment, I.5
  • 12
    • 0000033633 scopus 로고
    • Bacterial luciferase: Assay, purification and properties
    • Hastings J. W., Baldwin T. O., Nicoli M. Z. Bacterial luciferase: assay, purification and properties. Methods Enzymol. 57:1978;135-152.
    • (1978) Methods Enzymol. , vol.57 , pp. 135-152
    • Hastings, J.W.1    Baldwin, T.O.2    Nicoli, M.Z.3
  • 13
    • 0029653845 scopus 로고
    • Folding and association versus misfolding and aggregation of proteins
    • Jaenicke R. Folding and association versus misfolding and aggregation of proteins. Phil. Trans. Roy. Soc. London. 348:1995;97-105.
    • (1995) Phil. Trans. Roy. Soc. London , vol.348 , pp. 97-105
    • Jaenicke, R.1
  • 14
    • 0029757154 scopus 로고    scopus 로고
    • Influence of primary sequence transpositions on the folding pathways of ribonuclease T1
    • Johnson J. L., Raushel F. M. Influence of primary sequence transpositions on the folding pathways of ribonuclease T1. Biochemistry. 35:1996;10223-10233.
    • (1996) Biochemistry , vol.35 , pp. 10223-10233
    • Johnson, J.L.1    Raushel, F.M.2
  • 15
    • 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. 10:1996;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
  • 16
    • 0030756534 scopus 로고    scopus 로고
    • Protein memory through altered folding mediated by intramolecular chaperones
    • Shinde U. P., Liu J. J., Inouye M. Protein memory through altered folding mediated by intramolecular chaperones. Nature. 389:1997;520-522.
    • (1997) Nature , vol.389 , pp. 520-522
    • Shinde, U.P.1    Liu, J.J.2    Inouye, M.3
  • 17
    • 0024291671 scopus 로고
    • Effects of 3′ end deletions from the Vibrio harveyi luxB gene on luciferase subunit folding and enzyme assembly: Generation of temperature-sensitive polypeptide folding mutants
    • Sugihara J., Baldwin T. O. Effects of 3′ end deletions from the Vibrio harveyi luxB gene on luciferase subunit folding and enzyme assembly: generation of temperature-sensitive polypeptide folding mutants. Biochemistry. 27:1988;2872-2880.
    • (1988) Biochemistry , vol.27 , pp. 2872-2880
    • Sugihara, J.1    Baldwin, T.O.2
  • 18
    • 0022555882 scopus 로고
    • Complementation in folding and fragment exchange
    • Taniuchi H., Parr G. R., Juillerat M. A. Complementation in folding and fragment exchange. Methods Enzymol. 131:1986;185-217.
    • (1986) Methods Enzymol. , vol.131 , pp. 185-217
    • Taniuchi, H.1    Parr, G.R.2    Juillerat, M.A.3
  • 19
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera A. R., Blanco F. J., Serrano L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247:1995;670-681.
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 20
    • 0026476393 scopus 로고
    • The pro region of BPTI facilitates folding
    • Weissman J. S., Kim P. S. The pro region of BPTI facilitates folding. Cell. 71:1992;841-851.
    • (1992) Cell , vol.71 , pp. 841-851
    • Weissman, J.S.1    Kim, P.S.2
  • 21
    • 0027241972 scopus 로고
    • Refolding of luciferase subunits from urea and assembly of the active heterodimer
    • Ziegler M. M., Goldberg M. E., Chaffotte A. F., Baldwin T. O. Refolding of luciferase subunits from urea and assembly of the active heterodimer. J. Biol. Chem. 268:1993;10760-10765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10760-10765
    • Ziegler, M.M.1    Goldberg, M.E.2    Chaffotte, A.F.3    Baldwin, T.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.