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Volumn 474, Issue 7353, 2011, Pages 662-665

Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; IMMUNOGLOBULIN; PROTEIN;

EID: 79959830883     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10099     Document Type: Article
Times cited : (152)

References (37)
  • 3
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • DOI 10.1038/nature04195
    • Wright, C. F., Teichmann, S. A., Clarke, J. & Dobson, C. M. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438, 878-881 (2005). (Pubitemid 41753072)
    • (2005) Nature , vol.438 , Issue.7069 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 4
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescencemethods formolecular biology
    • Joo, C., Balci, H., Ishitsuka, Y., Buranachai, C. & Ha, T. Advances in single-molecule fluorescencemethods formolecular biology.Annu.Rev.Biochem.77, 51-76(2008).
    • (2008) Annu.Rev.Biochem. , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 5
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by single-molecule FRET
    • Schuler, B. & Eaton, W. A. Protein folding studied by single-molecule FRET. Curr. Opin. Struct. Biol. 18, 16-26 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 6
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • DOI 10.1074/jbc.272.52.32715
    • Fedorov, A. N. & Baldwin, T. O. Cotranslational protein folding. J. Biol. Chem. 272, 32715-32718 (1997). (Pubitemid 28023598)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.52 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 10
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846 (1978).
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 11
    • 67649856815 scopus 로고    scopus 로고
    • Direct single-molecule observation of a protein living in two opposed native structures
    • CrossRef.
    • Gambin, Y. et al. Direct single-molecule observation of a protein living in two opposed native structures. Proc. Natl Acad. Sci. USA 106, 10153-10158 (2009) CrossRef.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 10153-10158
    • Gambin, Y.1
  • 12
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • DOI 10.1016/S0969-2126(01)00596-2, PII S0969212601005962
    • Fowler, S. B. & Clarke, J. Mapping the folding pathway of an immunoglobulin domain: structural detail from phi value analysis and movement of the transition state. Structure 9, 355-366 (2001). (Pubitemid 32497263)
    • (2001) Structure , vol.9 , Issue.5 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 13
    • 77955360949 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of protein folding in a chaperonin cage
    • Hofmann, H. et al. Single-molecule spectroscopy of protein folding in a chaperonin cage. Proc. Natl Acad. Sci. USA 107, 11793-11798 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11793-11798
    • Hofmann, H.1
  • 14
    • 44049089395 scopus 로고    scopus 로고
    • Folding and misfolding in a naturally occurring circularly permuted PDZ domain
    • Ivarsson, Y., Travaglini-Allocatelli, C., Brunori, M. & Gianni, S. Folding and misfolding in a naturally occurring circularly permuted PDZ domain. J. Biol. Chem. 283, 8954-8960 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 8954-8960
    • Ivarsson, Y.1    Travaglini-Allocatelli, C.2    Brunori, M.3    Gianni, S.4
  • 15
    • 78649885501 scopus 로고    scopus 로고
    • Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain
    • Gianni, S. et al. Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain. Nature Struct. Mol. Biol. 17, 1431-1437 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1431-1437
    • Gianni, S.1
  • 16
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • Korzhnev, D. M., Religa, T. L., Banachewicz, W., Fersht, A. R. & Kay, L. E. A transient and low-populated protein-folding intermediate at atomic resolution. Science 329, 1312-1316 (2010).
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 17
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • DOI 10.1038/nsb757
    • Capaldi, A. P., Kleanthous, C. & Radford, S. E. Im7 folding mechanism: misfolding on a path to the native state. Nature Struct. Biol. 9, 209-216 (2002). (Pubitemid 34171314)
    • (2002) Nature Structural Biology , vol.9 , Issue.3 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 19
    • 33749519062 scopus 로고    scopus 로고
    • Folding mechanism of a multiple independently-folding domain protein: Double B domain of protein A
    • DOI 10.1021/bi060923s
    • Arora, P., Hammes, G. G. & Oas, T. G. Folding mechanism of a multiple independently-folding domain protein: double B domain of protein A. Biochemistry 45, 12312-12324 (2006). (Pubitemid 44527554)
    • (2006) Biochemistry , vol.45 , Issue.40 , pp. 12312-12324
    • Arora, P.1    Hammes, G.G.2    Oas, T.G.3
  • 20
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. Folding and association of proteins. Prog. Biophys. Mol. Biol. 49, 117-237 (1987).
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 21
    • 77951271571 scopus 로고    scopus 로고
    • Principles governing oligomer formation in amyloidogenic peptides
    • Straub, J. E. & Thirumalai, D. Principles governing oligomer formation in amyloidogenic peptides. Curr. Opin. Struct. Biol. 20, 187-195 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 187-195
    • Straub, J.E.1    Thirumalai, D.2
  • 22
    • 33646375442 scopus 로고    scopus 로고
    • Deposition Diseases and 3D Domain Swapping
    • DOI 10.1016/j.str.2006.03.011, PII S0969212606001791
    • Bennett, M. J., Sawaya, M. R. & Eisenberg, D. Deposition diseases and 3D domain swapping. Structure 14, 811-824 (2006). (Pubitemid 43674098)
    • (2006) Structure , vol.14 , Issue.5 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3
  • 23
    • 78650081316 scopus 로고    scopus 로고
    • Protein aggregation frominclusion bodies toamyloid and biomaterials
    • Mitraki, A. Protein aggregation frominclusion bodies toamyloid and biomaterials. Adv. Protein Chem. Struct. Biol. 79, 89-125 (2010).
    • (2010) Adv. Protein Chem. Struct. Biol. , vol.79 , pp. 89-125
    • Mitraki, A.1
  • 24
    • 52449107719 scopus 로고    scopus 로고
    • An effective strategy for the design of proteins with enhanced mechanical stability
    • Borgia, A., Steward, A. & Clarke, J. An effective strategy for the design of proteins with enhanced mechanical stability. Angew. Chem. Int. Ed. 47, 6900-6903 (2008).
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 6900-6903
    • Borgia, A.1    Steward, A.2    Clarke, J.3
  • 25
    • 52949145661 scopus 로고    scopus 로고
    • Recombination of protein fragments: A promising approach toward engineering proteins with novel nanomechanical properties
    • Balamurali, M. M. et al. Recombination of protein fragments: a promising approach toward engineering proteins with novel nanomechanical properties. Protein Sci. 17, 1815-1826 (2008).
    • (2008) Protein Sci. , vol.17 , pp. 1815-1826
    • Balamurali, M.M.1
  • 26
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., Isralewitz, B., Krammer, A., Vogel, V. & Schulten, K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75, 662-671 (1998). (Pubitemid 28357508)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 27
    • 84986512474 scopus 로고
    • CHARMM: Aprogramformacromolecular energy, minimization, and dynamics calculations
    • Brooks, B. R. et al.CHARMM: Aprogramformacromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 28
    • 0033444727 scopus 로고    scopus 로고
    • Ratiometric measurement and identification of single diffusing molecules
    • Dahan, M. et al. Ratiometric measurement and identification of single diffusing molecules. Chem. Phys. 247, 85-106 (1999).
    • (1999) Chem. Phys. , vol.247 , pp. 85-106
    • Dahan, M.1
  • 29
    • 0036304229 scopus 로고    scopus 로고
    • Titin; a multidomain protein that behaves as the sum of its parts
    • DOI 10.1006/jmbi.2001.5260
    • Scott, K. A., Steward, A., Fowler, S. B. & Clarke, J. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315, 819-829 (2002). (Pubitemid 34729329)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 30
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • DOI 10.1110/ps.0212702
    • Steward, A., Toca-Herrera, J. L. & Clarke, J. Versatile cloning systemfor construction of multimeric proteins for use in atomic force microscopy. Protein Sci. 11, 2179-2183 (2002). (Pubitemid 34919621)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 31
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • Schuler, B., Lipman, E. A. & Eaton, W. A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419, 743-747 (2002). (Pubitemid 35177962)
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 32
    • 73949104409 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins
    • Nettels, D. et al. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. Proc. Natl Acad. Sci. USA 106, 20740-20745 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20740-20745
    • Nettels, D.1
  • 33
    • 35948935175 scopus 로고    scopus 로고
    • Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy
    • DOI 10.1007/s10895-007-0187-z
    • Hillger, F., Nettels, D., Dorsch, S. & Schuler, B. Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy. J. Fluoresc. 17, 759-765 (2007). (Pubitemid 350075694)
    • (2007) Journal of Fluorescence , vol.17 , Issue.6 , pp. 759-765
    • Hillger, F.1    Nettels, D.2    Dorsch, S.3    Schuler, B.4
  • 34
    • 39049187155 scopus 로고    scopus 로고
    • Application of single molecule Förster resonance energy transfer to protein folding
    • (eds Bai, Y. & Nussinov, R.) (Humana Press
    • Schuler, B. Application of single molecule Förster resonance energy transfer to protein folding. Protein Folding Protocols (eds Bai, Y. & Nussinov, R.) 115-138 (Humana Press, 2007).
    • (2007) Protein Folding Protocols , pp. 115-138
    • Schuler, B.1
  • 36
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta, S., Politou, A. S. & Pastore, A. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure 4, 323-337 (1996).
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 37
    • 0242383943 scopus 로고    scopus 로고
    • Improved Go-like models demonstrate the robustness of protein folding mechanisms towards non-native interactions
    • DOI 10.1016/j.jmb.2003.09.047
    • Karanicolas, J. & Brooks, C. L. III. Improved Go-like models demonstrate the robustness of protein folding mechanisms towards non-native interactions. J. Mol. Biol. 334, 309-325 (2003). (Pubitemid 37357269)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.2 , pp. 309-325
    • Karanicolas, J.1    Brooks III, C.L.2


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