메뉴 건너뛰기




Volumn 585, Issue 12, 2011, Pages 1859-1863

Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers

Author keywords

In vitro transcription translation; Optical tweezers; Ribosome; Single molecule study

Indexed keywords

DOUBLE STRANDED DNA; POLYPEPTIDE; POLYSTYRENE;

EID: 79958177267     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.04.045     Document Type: Article
Times cited : (10)

References (30)
  • 2
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • DOI 10.1038/10754
    • J. Frydman, H. Erdjument-Bromage, P. Tempst, and F.U. Hartl Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase Nat. Struct. Biol. 6 1999 697 705 (Pubitemid 29318962)
    • (1999) Nature Structural Biology , vol.6 , Issue.7 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Ulrich Hartl, F.4
  • 3
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • V.A. Kolb, E.V. Makeyev, and A.S. Spirin Folding of firefly luciferase during translation in a cell-free system EMBO J. 13 1994 3631 3637 (Pubitemid 24246200)
    • (1994) EMBO Journal , vol.13 , Issue.15 , pp. 3631-3637
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 4
    • 0034595692 scopus 로고    scopus 로고
    • Co-translational folding of an eukaryotic multidomain protein in a prokaryotic translation system
    • DOI 10.1074/jbc.M002030200
    • V.A. Kolb, E.V. Makeyev, and A.S. Spirin Co-translational folding of an eukaryotic multidomain protein in a prokaryotic translation system J. Biol. Chem. 275 2000 16597 16601 (Pubitemid 30398885)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16597-16601
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 5
    • 22444436718 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of protein folding
    • DOI 10.1002/cphc.200400609
    • B. Schuler Single-molecule fluorescence spectroscopy of protein folding Chem. Phys. Chem. 6 2005 1206 1220 (Pubitemid 41008211)
    • (2005) ChemPhysChem , vol.6 , Issue.7 , pp. 1206-1220
    • Schuler, B.1
  • 7
    • 0038131090 scopus 로고    scopus 로고
    • Chain length dependence of apomyoglobin folding: Structural evolution from misfolded sheets to native helices
    • DOI 10.1021/bi0273056
    • C.C. Chow, C. Chow, V. Raghunathan, T.J. Huppert, E.B. Kimball, and S. Cavagnero Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices Biochemistry 42 2003 7090 7099 (Pubitemid 36706493)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7090-7099
    • Chow, C.C.1    Chow, C.2    Raghunathan, V.3    Huppert, T.J.4    Kimball, E.B.5    Cavagnero, S.6
  • 11
    • 33645033645 scopus 로고    scopus 로고
    • Probing gene expression in live cells, one protein molecule at a time
    • J. Yu, J. Xiao, X. Ren, K. Lao, and X.S. Xie Probing gene expression in live cells, one protein molecule at a time Science 311 2006 1600 1603
    • (2006) Science , vol.311 , pp. 1600-1603
    • Yu, J.1    Xiao, J.2    Ren, X.3    Lao, K.4    Xie, X.S.5
  • 14
    • 61349137508 scopus 로고    scopus 로고
    • Fast biosynthesis of GFP molecules: A single-molecule fluorescence study
    • A. Katranidis Fast biosynthesis of GFP molecules: a single-molecule fluorescence study Angew. Chem. Int. Ed. Engl. 48 2009 1758 1761
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 1758-1761
    • Katranidis, A.1
  • 16
    • 0024239966 scopus 로고
    • Parameters for the preparation of Escherichia coli ribosomes and ribosomal subunits active in tRNA binding
    • DOI 10.1016/S0076-6879(88)64076-6
    • H.J. Rheinberger, U. Geigenmuller, M. Wedde, and K.H. Nierhaus Parameters for the preparation of Escherichia coli ribosomes and ribosomal subunits active in tRNA binding Methods Enzymol. 164 1988 658 670 (Pubitemid 19067623)
    • (1988) Methods in Enzymology , vol.164 , pp. 658-670
    • Rheinberger, H.-J.1    Geigenmuller, U.2    Wedde, M.3    Nierhaus, K.H.4
  • 17
    • 0024166218 scopus 로고
    • +/polyamine system for polyuridine-dependent polyphenylalanine synthesis with near in vivo characteristics
    • DOI 10.1016/S0076-6879(88)64075-4
    • 4+/polyamine system for polyuridine-dependent polyphenylalanine synthesis with near in vivo characteristics Methods Enzymol. 164 1988 650 658 (Pubitemid 19067622)
    • (1988) Methods in Enzymology , vol.164 , pp. 650-658
    • Bartetzko, A.1    Nierhaus, K.H.2
  • 18
    • 0026342056 scopus 로고
    • Biosynthetic method for introducing unnatural amino acids site-specifically into proteins
    • J. Ellman, D. Mendel, S. Anthony-Cahill, C.J. Noren, and P.G. Schultz Biosynthetic method for introducing unnatural amino acids site-specifically into proteins Methods Enzymol. 202 1991 301 336
    • (1991) Methods Enzymol. , vol.202 , pp. 301-336
    • Ellman, J.1    Mendel, D.2    Anthony-Cahill, S.3    Noren, C.J.4    Schultz, P.G.5
  • 22
    • 0033506261 scopus 로고    scopus 로고
    • Ribosome display: An in vitro method for selection and evolution of antibodies from libraries
    • DOI 10.1016/S0022-1759(99)00149-0, PII S0022175999001490
    • C. Schaffitzel, J. Hanes, L. Jermutus, and A. Pluckthun Ribosome display: an in vitro method for selection and evolution of antibodies from libraries J. Immunol. Methods 231 1999 119 135 (Pubitemid 30394728)
    • (1999) Journal of Immunological Methods , vol.231 , Issue.1-2 , pp. 119-135
    • Schaffitzel, C.1    Hanes, J.2    Jermutus, L.3    Pluckthun, A.4
  • 23
    • 0036609104 scopus 로고    scopus 로고
    • Optical tweezers system measuring the change in light momentum flux
    • W. Grange, S. Husale, H.J. Guntherodt, and M. Hegner Optical tweezers system measuring the change in light momentum flux Rev. Sci. Instrum. 73 2002 2308 2316
    • (2002) Rev. Sci. Instrum. , vol.73 , pp. 2308-2316
    • Grange, W.1    Husale, S.2    Guntherodt, H.J.3    Hegner, M.4
  • 24
    • 0141521419 scopus 로고    scopus 로고
    • Protein synthesis by single ribosomes
    • DOI 10.1261/rna.5800303
    • F. Vanzi, S. Vladimirov, C.R. Knudsen, Y.E. Goldman, and B.S. Cooperman Protein synthesis by single ribosomes RNA 9 2003 1174 1179 (Pubitemid 37151672)
    • (2003) RNA , vol.9 , Issue.10 , pp. 1174-1179
    • Vanzi, F.1    Vladimirov, S.2    Knudsen, C.R.3    Goldman, Y.E.4    Cooperman, B.S.5
  • 25
    • 24144498660 scopus 로고    scopus 로고
    • Mechanical studies of single ribosome/mRNA complexes
    • DOI 10.1529/biophysj.104.056283
    • F. Vanzi, Y. Takagi, H. Shuman, B.S. Cooperman, and Y.E. Goldman Mechanical studies of single ribosome/mRNA complexes Biophys. J. 89 2005 1909 1919 (Pubitemid 41233546)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1909-1919
    • Vanzi, F.1    Takagi, Y.2    Shuman, H.3    Cooperman, B.S.4    Goldman, Y.E.5
  • 28
    • 33947501707 scopus 로고    scopus 로고
    • Peptide bond formation destabilizes Shine-Dalgarno interaction on the ribosome
    • DOI 10.1038/nature05625, PII NATURE05625
    • S. Uemura, M. Dorywalska, T.H. Lee, H.D. Kim, J.D. Puglisi, and S. Chu Peptide bond formation destabilizes Shine-Dalgarno interaction on the ribosome Nature 446 2007 454 457 (Pubitemid 46474601)
    • (2007) Nature , vol.446 , Issue.7134 , pp. 454-457
    • Uemura, S.1    Dorywalska, M.2    Lee, T.-H.3    Kim, H.D.4    Puglisi, J.D.5    Chu, S.6
  • 30
    • 0000920836 scopus 로고    scopus 로고
    • DNA handles for single molecule experiments
    • M. Hegner DNA handles for single molecule experiments Single Mol. 1 2000 139 144
    • (2000) Single Mol. , vol.1 , pp. 139-144
    • Hegner, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.