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Volumn 5, Issue 6, 2010, Pages 975-985

Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLYCINE; LIPASE B; MACROGOL; MALEIMIDE; N HYDROXYSUCCINIMIDE; THIOL; IMMOBILIZED ENZYME; IMMOBILIZED PROTEIN; MACROGOL DERIVATIVE; MALEIMIDE DERIVATIVE; N-HYDROXYSUCCINIMIDE; NUCLEIC ACID; SUCCINIMIDE DERIVATIVE; THIOL DERIVATIVE;

EID: 77952176659     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2010.49     Document Type: Article
Times cited : (134)

References (34)
  • 1
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • DOI 10.1016/S0092-8674(00)80911-3
    • Ishijima, A. et al. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-171 (1998). (Pubitemid 28073040)
    • (1998) Cell , vol.92 , Issue.2 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 2
    • 17444366080 scopus 로고    scopus 로고
    • Simultaneous coincident optical trapping and single-molecule fluorescence
    • Lang, M.J., Fordyce, P.M., Engh, A.M., Neuman, K.C. & Block, S.M. Simultaneous, coincident optical trapping and single-molecule fluorescence. Nat. Methods 1, 133-139 (2004).
    • (2004) Nat. Methods , vol.1 , pp. 133-139
    • Lang, M.J.1    Fordyce, P.M.2    Engh, A.M.3    Neuman, K.C.4    Block, S.M.5
  • 3
    • 13644273766 scopus 로고    scopus 로고
    • Mechanical perturbationinduced fluorescence change of green fluorescent protein
    • Kodama, T., Ohtani, H., Arakawa, H. & Ikai, A. Mechanical perturbationinduced fluorescence change of green fluorescent protein. Appl. Phys. Lett. 86, 043901 (2005).
    • (2005) Appl. Phys. Lett. , vol.86 , pp. 043901
    • Kodama, T.1    Ohtani, H.2    Arakawa, H.3    Ikai, A.4
  • 4
    • 33745699041 scopus 로고    scopus 로고
    • An integrated instrumental setup for the combination of atomic force microscopy with optical spectroscopy
    • DOI 10.1002/bip.20414
    • Owen, R.J., Heyes, C.D., Knebel, D., Rocker, C. & Nienhaus, G.U. An integrated instrumental setup for the combination of atomic force microscopy with optical spectroscopy. Biopolymers 82, 410-414 (2006). (Pubitemid 44000914)
    • (2006) Biopolymers , vol.82 , Issue.4 , pp. 410-414
    • Owen, R.J.1    Heyes, C.D.2    Knebel, D.3    Rocker, C.4    Nienhaus, G.U.5
  • 6
    • 67650318292 scopus 로고    scopus 로고
    • Ultrastable combined atomic force and total internal fluorescence microscope
    • Gumpp, H., Stahl, S.W., Strackharn, M., Puchner, E.M. & Gaub, H.E. Ultrastable combined atomic force and total internal fluorescence microscope. Rev. Sci. Instrum. 80, 063704 (2009).
    • (2009) Rev. Sci. Instrum. , vol.80 , pp. 063704
    • Gumpp, H.1    Stahl, S.W.2    Strackharn, M.3    Puchner, E.M.4    Gaub, H.E.5
  • 7
    • 58149254174 scopus 로고    scopus 로고
    • Nanoparticle self-assembly on a DNA-scaffold written by single-molecule cut-and-paste
    • Puchner, E.M., Kufer, S.K., Strackharn, M., Stahl, S.W. & Gaub, H.E. Nanoparticle self-assembly on a DNA-scaffold written by single-molecule cut-and-paste. Nano Lett. 8, 3692-3695 (2008).
    • (2008) Nano Lett , vol.8 , pp. 3692-3695
    • Puchner, E.M.1    Kufer, S.K.2    Strackharn, M.3    Stahl, S.W.4    Gaub, H.E.5
  • 8
    • 58149263195 scopus 로고    scopus 로고
    • Optically monitoring the mechanical assembly of single molecules
    • Kufer, S.K. et al. Optically monitoring the mechanical assembly of single molecules. Nat. Nanotechnol. 4, 45-49 (2009).
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 45-49
    • Kufer, S.K.1
  • 9
    • 70349961707 scopus 로고    scopus 로고
    • Triggering enzymatic activity with force
    • Gumpp, H. et al. Triggering enzymatic activity with force. Nano Lett. 9, 3290-3295 (2009).
    • (2009) Nano Lett , vol.9 , pp. 3290-3295
    • Gumpp, H.1
  • 10
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P. & Dufrene, Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3, 347-355 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 11
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • Roy, R., Hohng, S. & Ha, T. A practical guide to single-molecule FRET. Nat. Methods 5, 507-516 (2008). (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 13
    • 33646679654 scopus 로고    scopus 로고
    • Michael addition reactions in macromolecular design for emerging technologies
    • DOI 10.1016/j.progpolymsci.2006.03.001, PII S0079670006000335
    • Mather, B.D., Viswanathan, K., Miller, K.M. & Long, T.E. Michael addition reactions in macromolecular design for emerging technologies. Prog. Polym. Sci. 31, 487-531 (2006). (Pubitemid 43737245)
    • (2006) Progress in Polymer Science (Oxford) , vol.31 , Issue.5 , pp. 487-531
    • Mather, B.D.1    Viswanathan, K.2    Miller, K.M.3    Long, T.E.4
  • 14
    • 0001832838 scopus 로고    scopus 로고
    • Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water
    • PII S1367263099991218
    • Oesterhelt, F., Rief, M. & Gaub, H.E. Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water. New J. Phys. 1, 6.1-6.11 (1999). (Pubitemid 38871123)
    • (1999) New Journal of Physics , vol.1 , pp. 61-611
    • Oesterhelt, F.1    Rief, M.2    Gaub, H.E.3
  • 16
    • 0026122420 scopus 로고
    • Protein surface interactions in the presence of polyethylene oxide. 1. Simplified theory
    • Jeon, S.I., Lee, J.H., Andrade, J.D. & Degennes, P.G. Protein surface interactions in the presence of polyethylene oxide. 1. Simplified theory. J. Colloid Interface Sci. 142, 149-158 (1991).
    • (1991) J. Colloid Interface Sci. , vol.142 , pp. 149-158
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    Degennes, P.G.4
  • 17
    • 0346540564 scopus 로고    scopus 로고
    • Protein Adsorption on Poly(ethylene oxide)-Grafted Silicon Surfaces
    • Sofia, S.J. & Merrill, E.W. Protein adsorption on poly(ethylene oxide)- grafted silicon surfaces. In Poly(ethylene glycol) Chemistry and Biological Applications (eds. Harris J.M. & Zalipsky, S.) Ch. 22, 342-360 (ACS Symposium Series, Washington, D.C., 1997). (Pubitemid 127444776)
    • (1997) ACS Symposium Series , vol.680 , pp. 342-360
    • Sofia, S.J.1    Merrill, E.W.2
  • 19
    • 34447632456 scopus 로고    scopus 로고
    • Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers
    • DOI 10.1016/j.ultramic.2007.02.035, PII S0304399107001040
    • Ebner, A., Hinterdorfer, P. & Gruber, H.J. Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers. Ultramicroscopy 107, 922-927 (2007). (Pubitemid 47095101)
    • (2007) Ultramicroscopy , vol.107 , Issue.10-11 , pp. 922-927
    • Ebner, A.1    Hinterdorfer, P.2    Gruber, H.J.3
  • 21
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labelling and sensing
    • DOI 10.1038/nmat1390
    • Medintz, I.L., Uyeda, H.T., Goldman, E.R. & Mattoussi, H. Quantum dot bioconjugates for imaging, labelling and sensing. Nat. Mater. 4, 435-446 (2005). (Pubitemid 40774047)
    • (2005) Nature Materials , vol.4 , Issue.6 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 22
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • DOI 10.1021/bm061197b
    • Rusmini, F., Zhong, Z. & Feijen, J. Protein immobilization strategies for protein biochips. Biomacromolecules 8, 1775-1789 (2007). (Pubitemid 47009952)
    • (2007) Biomacromolecules , vol.8 , Issue.6 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 24
    • 58149260099 scopus 로고    scopus 로고
    • Biosensors and tools for surface functionalization from the macro-to the nanoscale: The way forward
    • Nicu, L. & Leichle, T. Biosensors and tools for surface functionalization from the macro-to the nanoscale: The way forward. J. Appl. Phys. 104, 111101 (2008).
    • (2008) J. Appl. Phys. , vol.104 , pp. 111101
    • Nicu, L.1    Leichle, T.2
  • 25
    • 0001153517 scopus 로고
    • Selective reduction of disulfides by Tris(2-carboxyethyl)phosphine
    • Burns, J.A., Butler, J.C., Moran, J. & Whitesides, G.M. Selective reduction of disulfides by Tris(2-carboxyethyl)phosphine. J. Org. Chem. 56, 2648-2650 (1991).
    • (1991) J. Org. Chem. , vol.56 , pp. 2648-2650
    • Burns, J.A.1    Butler, J.C.2    Moran, J.3    Whitesides, G.M.4
  • 26
    • 33748578351 scopus 로고    scopus 로고
    • Site-specific immobilization of genetically engineered variants of Candida antarctica lipase B
    • DOI 10.1002/cbic.200600198
    • Blank, K., Morfill, J. & Gaub, H.E. Site-specific immobilization of genetically engineered variants of Candida antarctica lipase B. Chembiochem 7, 1349-1351 (2006). (Pubitemid 44369085)
    • (2006) ChemBioChem , vol.7 , Issue.9 , pp. 1349-1351
    • Blank, K.1    Morfill, J.2    Gaub, H.E.3
  • 27
    • 48749094946 scopus 로고    scopus 로고
    • Force-based analysis of multidimensional energy landscapes: Application of dynamic force spectroscopy and steered molecular dynamics simulations to an antibody fragment-peptide complex
    • Morfill, J. et al. Force-based analysis of multidimensional energy landscapes: application of dynamic force spectroscopy and steered molecular dynamics simulations to an antibody fragment-peptide complex. J. Mol. Biol. 381, 1253-1266 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 1253-1266
    • Morfill, J.1
  • 30
    • 0028073310 scopus 로고
    • An improved affinity tag based on the FLAG® peptide for the detection and purification of recombinant antibody fragments
    • Knappik, A. & Plückthun, A. An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. Biotechniques 17, 754-761 (1994). (Pubitemid 24313442)
    • (1994) BioTechniques , vol.17 , Issue.4 , pp. 754-761
    • Knappik, A.1    Pluckthun, A.2
  • 31
    • 2442442119 scopus 로고    scopus 로고
    • Directed in Vitro Evolution and Crystallographic Analysis of a Peptide-binding Single Chain Antibody Fragment (scFv) with Low Picomolar Affinity
    • DOI 10.1074/jbc.M309169200
    • Zahnd, C. et al. Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity. J. Biol. Chem. 279, 18870-18877 (2004). (Pubitemid 38623314)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18870-18877
    • Zahnd, C.1    Spinelli, S.2    Luginbuhl, B.3    Amstutz, P.4    Cambillau, C.5    Pluckthun, A.6
  • 34
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • DOI 10.1016/j.febslet.2005.12.052, PII S0014579305015358
    • Neuert, G., Albrecht, C., Pamir, E. & Gaub, H.E. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580, 505-509 (2006). (Pubitemid 43089679)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4


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